JP3913787B2 - I型コラーゲン断片のサンドウイッチ測定法 - Google Patents
I型コラーゲン断片のサンドウイッチ測定法 Download PDFInfo
- Publication number
- JP3913787B2 JP3913787B2 JP52618698A JP52618698A JP3913787B2 JP 3913787 B2 JP3913787 B2 JP 3913787B2 JP 52618698 A JP52618698 A JP 52618698A JP 52618698 A JP52618698 A JP 52618698A JP 3913787 B2 JP3913787 B2 JP 3913787B2
- Authority
- JP
- Japan
- Prior art keywords
- collagen
- assay
- antibody
- amino acid
- epitope
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 239000012634 fragment Substances 0.000 title claims description 62
- 238000003556 assay Methods 0.000 title claims description 42
- 108010022452 Collagen Type I Proteins 0.000 title claims description 14
- 102000012422 Collagen Type I Human genes 0.000 title claims description 14
- 229920001436 collagen Polymers 0.000 claims abstract description 77
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract description 23
- 230000011382 collagen catabolic process Effects 0.000 claims abstract description 20
- 102000008186 Collagen Human genes 0.000 claims description 77
- 108010035532 Collagen Proteins 0.000 claims description 77
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 57
- 238000000034 method Methods 0.000 claims description 52
- 150000001413 amino acids Chemical class 0.000 claims description 21
- 239000007857 degradation product Substances 0.000 claims description 9
- 238000001727 in vivo Methods 0.000 claims description 5
- 230000001900 immune effect Effects 0.000 claims description 4
- 238000010521 absorption reaction Methods 0.000 claims description 2
- 238000003127 radioimmunoassay Methods 0.000 claims 1
- 238000003118 sandwich ELISA Methods 0.000 claims 1
- 238000003018 immunoassay Methods 0.000 abstract description 5
- 210000000988 bone and bone Anatomy 0.000 description 23
- 229940024606 amino acid Drugs 0.000 description 21
- 239000000427 antigen Substances 0.000 description 21
- 102000036639 antigens Human genes 0.000 description 21
- 108091007433 antigens Proteins 0.000 description 21
- 235000001014 amino acid Nutrition 0.000 description 20
- 210000002966 serum Anatomy 0.000 description 20
- 241000282414 Homo sapiens Species 0.000 description 18
- 102000004196 processed proteins & peptides Human genes 0.000 description 18
- 210000002700 urine Anatomy 0.000 description 17
- 210000001124 body fluid Anatomy 0.000 description 16
- 239000010839 body fluid Substances 0.000 description 16
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 15
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 15
- 229960002591 hydroxyproline Drugs 0.000 description 15
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 15
- 208000006386 Bone Resorption Diseases 0.000 description 13
- 230000024279 bone resorption Effects 0.000 description 13
- 230000015556 catabolic process Effects 0.000 description 11
- 239000000243 solution Substances 0.000 description 10
- 238000006731 degradation reaction Methods 0.000 description 9
- 230000003053 immunization Effects 0.000 description 9
- 210000001519 tissue Anatomy 0.000 description 9
- 230000002485 urinary effect Effects 0.000 description 9
- CKLJMWTZIZZHCS-UWTATZPHSA-N D-aspartic acid Chemical compound OC(=O)[C@H](N)CC(O)=O CKLJMWTZIZZHCS-UWTATZPHSA-N 0.000 description 8
- 208000001132 Osteoporosis Diseases 0.000 description 8
- 201000010099 disease Diseases 0.000 description 8
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 8
- 238000002649 immunization Methods 0.000 description 8
- 235000018102 proteins Nutrition 0.000 description 8
- 102000004169 proteins and genes Human genes 0.000 description 8
- 108090000623 proteins and genes Proteins 0.000 description 8
- 241000894007 species Species 0.000 description 8
- 239000000758 substrate Substances 0.000 description 8
- GRFNBEZIAWKNCO-UHFFFAOYSA-N 3-pyridinol Chemical group OC1=CC=CN=C1 GRFNBEZIAWKNCO-UHFFFAOYSA-N 0.000 description 7
- 102000001187 Collagen Type III Human genes 0.000 description 7
- 108010069502 Collagen Type III Proteins 0.000 description 7
- 238000002965 ELISA Methods 0.000 description 7
- 230000000692 anti-sense effect Effects 0.000 description 7
- 238000004132 cross linking Methods 0.000 description 7
- 238000005259 measurement Methods 0.000 description 7
- 206010065687 Bone loss Diseases 0.000 description 6
- 102000029816 Collagenase Human genes 0.000 description 6
- 108060005980 Collagenase Proteins 0.000 description 6
- 208000010191 Osteitis Deformans Diseases 0.000 description 6
- 208000027868 Paget disease Diseases 0.000 description 6
- 239000002671 adjuvant Substances 0.000 description 6
- 150000001299 aldehydes Chemical class 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 210000004027 cell Anatomy 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 6
- 229960002424 collagenase Drugs 0.000 description 6
- 238000000502 dialysis Methods 0.000 description 6
- 108010045624 glutamyl-lysyl-alanyl-histidyl-aspartyl-glycyl-glycyl-arginine Proteins 0.000 description 6
- 238000006317 isomerization reaction Methods 0.000 description 6
- 208000027202 mammary Paget disease Diseases 0.000 description 6
- 229960005261 aspartic acid Drugs 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 238000004519 manufacturing process Methods 0.000 description 5
- 102000013415 peroxidase activity proteins Human genes 0.000 description 5
- 108040007629 peroxidase activity proteins Proteins 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 239000007787 solid Substances 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 4
- 206010020100 Hip fracture Diseases 0.000 description 4
- 241001465754 Metazoa Species 0.000 description 4
- 108010033276 Peptide Fragments Proteins 0.000 description 4
- 102000007079 Peptide Fragments Human genes 0.000 description 4
- 108010050808 Procollagen Proteins 0.000 description 4
- LCYXYLLJXMAEMT-SAXRGWBVSA-N Pyridinoline Chemical compound OC(=O)[C@@H](N)CCC1=C[N+](C[C@H](O)CC[C@H](N)C([O-])=O)=CC(O)=C1C[C@H](N)C(O)=O LCYXYLLJXMAEMT-SAXRGWBVSA-N 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 108010090804 Streptavidin Proteins 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 4
- 235000003704 aspartic acid Nutrition 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N aspartic acid group Chemical group N[C@@H](CC(=O)O)C(=O)O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 4
- 230000007691 collagen metabolic process Effects 0.000 description 4
- 229940096422 collagen type i Drugs 0.000 description 4
- YSMODUONRAFBET-UHNVWZDZSA-N erythro-5-hydroxy-L-lysine Chemical group NC[C@H](O)CC[C@H](N)C(O)=O YSMODUONRAFBET-UHNVWZDZSA-N 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 102000000503 Collagen Type II Human genes 0.000 description 3
- 108010041390 Collagen Type II Proteins 0.000 description 3
- ZAHDXEIQWWLQQL-IHRRRGAJSA-N Deoxypyridinoline Chemical compound OC(=O)[C@@H](N)CCCC[N+]1=CC(O)=C(C[C@H](N)C([O-])=O)C(CC[C@H](N)C(O)=O)=C1 ZAHDXEIQWWLQQL-IHRRRGAJSA-N 0.000 description 3
- 206010017076 Fracture Diseases 0.000 description 3
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 3
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 241000283973 Oryctolagus cuniculus Species 0.000 description 3
- 108090000573 Osteocalcin Proteins 0.000 description 3
- 108010034949 Thyroglobulin Proteins 0.000 description 3
- 102000009843 Thyroglobulin Human genes 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 150000001718 carbodiimides Chemical class 0.000 description 3
- 238000004113 cell culture Methods 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 238000012875 competitive assay Methods 0.000 description 3
- 230000021615 conjugation Effects 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 239000000835 fiber Substances 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 229960002175 thyroglobulin Drugs 0.000 description 3
- 238000011282 treatment Methods 0.000 description 3
- -1 1:1-29 Proteins 0.000 description 2
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- CKLJMWTZIZZHCS-UHFFFAOYSA-N D-OH-Asp Natural products OC(=O)C(N)CC(O)=O CKLJMWTZIZZHCS-UHFFFAOYSA-N 0.000 description 2
- 102000010834 Extracellular Matrix Proteins Human genes 0.000 description 2
- 108010037362 Extracellular Matrix Proteins Proteins 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 208000030136 Marchiafava-Bignami Disease Diseases 0.000 description 2
- 208000001826 Marfan syndrome Diseases 0.000 description 2
- 208000029725 Metabolic bone disease Diseases 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 102000004067 Osteocalcin Human genes 0.000 description 2
- 206010031243 Osteogenesis imperfecta Diseases 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 229920001213 Polysorbate 20 Polymers 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 230000000890 antigenic effect Effects 0.000 description 2
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 2
- 239000012131 assay buffer Substances 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 239000013060 biological fluid Substances 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 238000011088 calibration curve Methods 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 150000001732 carboxylic acid derivatives Chemical class 0.000 description 2
- 239000003593 chromogenic compound Substances 0.000 description 2
- 230000003366 colagenolytic effect Effects 0.000 description 2
- 210000002808 connective tissue Anatomy 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 210000002744 extracellular matrix Anatomy 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 230000002503 metabolic effect Effects 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 230000001613 neoplastic effect Effects 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 150000007523 nucleic acids Chemical class 0.000 description 2
- 201000008482 osteoarthritis Diseases 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 2
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 2
- 230000035755 proliferation Effects 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 239000012465 retentate Substances 0.000 description 2
- 206010039073 rheumatoid arthritis Diseases 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 210000004989 spleen cell Anatomy 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- UVGHPGOONBRLCX-NJSLBKSFSA-N (2,5-dioxopyrrolidin-1-yl) 6-[5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]pentanoylamino]hexanoate Chemical compound C([C@H]1[C@H]2NC(=O)N[C@H]2CS1)CCCC(=O)NCCCCCC(=O)ON1C(=O)CCC1=O UVGHPGOONBRLCX-NJSLBKSFSA-N 0.000 description 1
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 1
- 201000000736 Amenorrhea Diseases 0.000 description 1
- 206010001928 Amenorrhoea Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- ZMOUVWHDCOZPGR-UHFFFAOYSA-N BNBr Chemical group BNBr ZMOUVWHDCOZPGR-UHFFFAOYSA-N 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 208000020084 Bone disease Diseases 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 101800001415 Bri23 peptide Proteins 0.000 description 1
- 101800000655 C-terminal peptide Proteins 0.000 description 1
- 102400000107 C-terminal peptide Human genes 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 102100036213 Collagen alpha-2(I) chain Human genes 0.000 description 1
- 206010010214 Compression fracture Diseases 0.000 description 1
- 206010013883 Dwarfism Diseases 0.000 description 1
- 102000016942 Elastin Human genes 0.000 description 1
- 108010014258 Elastin Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000875067 Homo sapiens Collagen alpha-2(I) chain Proteins 0.000 description 1
- LCWXJXMHJVIJFK-UHFFFAOYSA-N Hydroxylysine Natural products NCC(O)CC(N)CC(O)=O LCWXJXMHJVIJFK-UHFFFAOYSA-N 0.000 description 1
- 201000002980 Hyperparathyroidism Diseases 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 208000012659 Joint disease Diseases 0.000 description 1
- 102100031475 Osteocalcin Human genes 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 229920001030 Polyethylene Glycol 4000 Polymers 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 101000933967 Pseudomonas phage KPP25 Major capsid protein Proteins 0.000 description 1
- 208000025747 Rheumatic disease Diseases 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 206010047115 Vasculitis Diseases 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000004520 agglutination Effects 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 231100000540 amenorrhea Toxicity 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 238000011444 antiresorptive therapy Methods 0.000 description 1
- 210000001188 articular cartilage Anatomy 0.000 description 1
- 238000002820 assay format Methods 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 230000006287 biotinylation Effects 0.000 description 1
- 238000007413 biotinylation Methods 0.000 description 1
- 208000034158 bleeding Diseases 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 230000010072 bone remodeling Effects 0.000 description 1
- 230000008416 bone turnover Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 108091006116 chimeric peptides Proteins 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 108010049937 collagen type I trimeric cross-linked peptide Proteins 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 238000002967 competitive immunoassay Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- 239000012531 culture fluid Substances 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- YSMODUONRAFBET-UHFFFAOYSA-N delta-DL-hydroxylysine Natural products NCC(O)CCC(N)C(O)=O YSMODUONRAFBET-UHFFFAOYSA-N 0.000 description 1
- 238000000326 densiometry Methods 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229920002549 elastin Polymers 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 210000003722 extracellular fluid Anatomy 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 238000001215 fluorescent labelling Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- 230000001744 histochemical effect Effects 0.000 description 1
- 210000004754 hybrid cell Anatomy 0.000 description 1
- QJHBJHUKURJDLG-UHFFFAOYSA-N hydroxy-L-lysine Natural products NCCCCC(NO)C(O)=O QJHBJHUKURJDLG-UHFFFAOYSA-N 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000011532 immunohistochemical staining Methods 0.000 description 1
- 238000010324 immunological assay Methods 0.000 description 1
- 230000003308 immunostimulating effect Effects 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 239000007928 intraperitoneal injection Substances 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 239000004816 latex Substances 0.000 description 1
- 229920000126 latex Polymers 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 230000009245 menopause Effects 0.000 description 1
- 208000030159 metabolic disease Diseases 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 230000001394 metastastic effect Effects 0.000 description 1
- 206010061289 metastatic neoplasm Diseases 0.000 description 1
- 239000011325 microbead Substances 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 210000004898 n-terminal fragment Anatomy 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 230000000474 nursing effect Effects 0.000 description 1
- 230000011164 ossification Effects 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- KHIWWQKSHDUIBK-UHFFFAOYSA-N periodic acid Chemical compound OI(=O)(=O)=O KHIWWQKSHDUIBK-UHFFFAOYSA-N 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 238000010791 quenching Methods 0.000 description 1
- 230000000171 quenching effect Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 208000037974 severe injury Diseases 0.000 description 1
- 230000009528 severe injury Effects 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000012086 standard solution Substances 0.000 description 1
- 238000011146 sterile filtration Methods 0.000 description 1
- 239000012089 stop solution Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 208000011580 syndromic disease Diseases 0.000 description 1
- 210000001179 synovial fluid Anatomy 0.000 description 1
- 229960000814 tetanus toxoid Drugs 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 230000003156 vasculitic effect Effects 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
Images
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/543—Immunoassay; Biospecific binding assay; Materials therefor with an insoluble carrier for immobilising immunochemicals
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6887—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids from muscle, cartilage or connective tissue
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2800/00—Detection or diagnosis of diseases
- G01N2800/10—Musculoskeletal or connective tissue disorders
- G01N2800/108—Osteoporosis
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S436/00—Chemistry: analytical and immunological testing
- Y10S436/815—Test for named compound or class of compounds
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Chemical & Material Sciences (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Food Science & Technology (AREA)
- General Physics & Mathematics (AREA)
- Cell Biology (AREA)
- Biotechnology (AREA)
- Medicinal Chemistry (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Pathology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Paints Or Removers (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GBGB9625559.1A GB9625559D0 (en) | 1996-12-09 | 1996-12-09 | Sandwish assays for collagen type I fragments |
| GB9625559.1 | 1997-03-19 | ||
| GBGB9705687.3A GB9705687D0 (en) | 1997-03-19 | 1997-03-19 | Sandwich assays for collagen type i fragments |
| GB9705687.3 | 1997-03-19 | ||
| PCT/EP1997/006803 WO1998026286A2 (en) | 1996-12-09 | 1997-12-05 | Sandwich assays for collagen type i fragments |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2001506000A JP2001506000A (ja) | 2001-05-08 |
| JP2001506000A5 JP2001506000A5 (enExample) | 2005-07-14 |
| JP3913787B2 true JP3913787B2 (ja) | 2007-05-09 |
Family
ID=26310589
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP52618698A Expired - Fee Related JP3913787B2 (ja) | 1996-12-09 | 1997-12-05 | I型コラーゲン断片のサンドウイッチ測定法 |
Country Status (8)
| Country | Link |
|---|---|
| US (2) | US6660481B2 (enExample) |
| EP (1) | EP0944833B1 (enExample) |
| JP (1) | JP3913787B2 (enExample) |
| AT (1) | ATE202632T1 (enExample) |
| AU (1) | AU5754298A (enExample) |
| DE (1) | DE69705423T2 (enExample) |
| ES (1) | ES2160985T3 (enExample) |
| WO (1) | WO1998026286A2 (enExample) |
Families Citing this family (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5962639A (en) * | 1987-11-06 | 1999-10-05 | Washington Research Foundation | Synthetic peptides corresponding to telopeptide sequences of cross-linked type I collagen metabolites |
| DE69705423T2 (de) * | 1996-12-09 | 2002-05-16 | Osteometer Biotech As Herlev | Sandwichtest zum nachweis von kollagenfragmenten |
| GB9928052D0 (en) * | 1999-11-26 | 2000-01-26 | Osteometer Biotech As | Assay of isomerised and/or optically inverted proteins and protein fragments |
| US7354723B2 (en) | 1999-11-26 | 2008-04-08 | Nordic Bioscience Dagnostics A/S | Assay of isomerised and/or optically inverted proteins and protein fragments |
| AU2001276395A1 (en) * | 2000-07-12 | 2002-02-05 | Werner Naser | Direct assessment of relative concentrations of variants of an epitope on a dimeric molecule |
| EP2287330A1 (en) * | 2001-11-01 | 2011-02-23 | Rensselaer Polytechnic Institute | Biocatalytic Solgel Microarrays |
| US20050124071A1 (en) * | 2003-09-30 | 2005-06-09 | Kraus Virginia B. | Methods and compositions for diagnosing musculoskeletal, arthritic and joint disorders by biomarker dating |
| CA2628219C (en) * | 2005-11-01 | 2012-11-27 | Rensselaer Polytechnic Institute | Three-dimensional cellular array chip and platform for toxicology assays |
| WO2009038771A2 (en) * | 2007-09-19 | 2009-03-26 | Massachusetts Institute Of Technology | Tolperisone and tolperisone-like drugs for the treatment of k-ras associated cancers |
| US20110281279A1 (en) * | 2007-12-21 | 2011-11-17 | Siemens Healthcare Diagnostics Inc. | CIRCULATING Epha2 RECEPTOR |
| US8796184B2 (en) | 2008-03-28 | 2014-08-05 | Sentilus, Inc. | Detection assay devices and methods of making and using the same |
| WO2013158217A1 (en) * | 2012-04-20 | 2013-10-24 | Thomas Jefferson University | Engineered antibody for inhibition of fibrosis |
| US9753030B2 (en) * | 2013-03-06 | 2017-09-05 | University of Pittsburgh—of the Commonwealth System of Higher Education | Degradable carbon nanotube-containing biosensors and methods for target clinical marker detection |
| ES2687220B1 (es) * | 2017-03-23 | 2019-08-08 | Servicio Andaluz De Salud | Método de obtención de datos útiles para el cribado y diagnóstico de la osteoporosis |
| WO2022202876A1 (ja) * | 2021-03-24 | 2022-09-29 | 積水メディカル株式会社 | I型コラーゲンc末端テロペプチドの免疫学的分析方法 |
| WO2023068249A1 (ja) * | 2021-10-20 | 2023-04-27 | 積水メディカル株式会社 | I型コラーゲン架橋n-テロペプチドの測定試薬、その調製方法、及びそれを用いた免疫測定方法 |
Family Cites Families (39)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NL6716836A (enExample) | 1967-12-11 | 1969-06-13 | ||
| DE2816841A1 (de) | 1978-04-18 | 1979-10-31 | Max Planck Gesellschaft | Radioimmunologische bestimmung von prokollagen (typ iii) und prokollagen- peptid (typ iii) |
| US4376110A (en) * | 1980-08-04 | 1983-03-08 | Hybritech, Incorporated | Immunometric assays using monoclonal antibodies |
| DE3209149A1 (de) | 1982-03-13 | 1983-10-06 | Hoechst Ag | Verfahren zur gemeinsamen immunologischen bestimmung von prokollagen-peptid (typ iii) und prokollagen-peptid col 1 (typ iii) und verfahren zur herstellung von anti-prokollagen-peptid col 1 (typ iii)-serum |
| US4628027A (en) | 1982-05-19 | 1986-12-09 | Molecular Engineering Associates, Ltd. | Vitro diagnostic methods using monoclonal antibodies against connective tissue proteins |
| CA1251729A (en) | 1982-05-19 | 1989-03-28 | Steffen Gay | In vitro diagnostic methods using monoclonal antibodies against connective tissue proteins |
| SE8304836D0 (sv) | 1983-09-09 | 1983-09-09 | Pharmacia Ab | Sett att bestemma forendringar i ledbrosk |
| US5001225A (en) | 1986-12-08 | 1991-03-19 | Georgetown University | Monoclonal antibodies to a pan-malarial antigen |
| JPS63209318A (ja) | 1987-02-26 | 1988-08-30 | Sony Corp | 受信機 |
| US5679583A (en) | 1987-05-02 | 1997-10-21 | Hoechst Aktiengesellschaft | Monoclonal antibodies for the selective immunological determination of intact procollagen peptide (type III) and procollagen (type III) in body fluids |
| DE3714634A1 (de) | 1987-05-02 | 1988-11-17 | Hoechst Ag | Verfahren zur selektiven immunologischen bestimmung von intaktem prokollagen peptid (typ iii) und prokollagen (typ iii) in koerperfluessigkeiten und mittel zu dessen durchfuehrung |
| GB2205643B (en) | 1987-05-08 | 1991-03-13 | Farmos Group Limited | Type iii collagen degradation assay |
| US5320970A (en) | 1987-11-06 | 1994-06-14 | Washington Research Foundation | Detection of collagen degradation in vivo |
| US4973666A (en) | 1987-11-06 | 1990-11-27 | Washington Research Foundation | Peptide fragments containing HP and LP cross-links |
| US5300434A (en) | 1987-11-06 | 1994-04-05 | Washington Research Foundation | Hybridoma cell line producing an antibody to type-I collagen amino-terminal telopeptide |
| ATE115963T1 (de) | 1988-04-27 | 1995-01-15 | Hoechst Ag | Monoklonaler antikörper zur selektiven immunologischen bestimmung von intaktem prokollagen peptid (typ iii) und prokollagen (typ iii) in körperflüssigkeiten. |
| GB8815174D0 (en) | 1988-06-25 | 1988-08-03 | Rowett Research Inst | Method of monitoring collagen degradation |
| WO1990004417A1 (en) | 1988-10-24 | 1990-05-03 | Bruce Caterson | Methods of and compositions for diagnosing, monitoring and treating the early stages of osteoarthritis |
| WO1990008195A1 (en) | 1989-01-13 | 1990-07-26 | President And Fellows Of Harvard College | Monoclonal antibody to human type ix collagen |
| ZA909755B (en) | 1989-12-07 | 1991-09-25 | Res Dev Foundation | Cell cycle-dependent regulation of phosphorylation of the human retinoblastoma gene product |
| GB9014220D0 (en) | 1990-06-26 | 1990-08-15 | Farmos Yhtymy Oy | Method for the immunlolgical determinition of the carboxyterminal propeptide of type i procollagen |
| GB9105893D0 (en) | 1991-03-20 | 1991-05-08 | Orion Yhtymae Oy | Bone resorption assay based on a peptide liberated during collagen degradation |
| DE4225038C2 (de) | 1992-07-29 | 1995-11-30 | Boehringer Mannheim Gmbh | Herstellung und Verwendung von Antikörpern gegen Kollagen |
| DE69333641T2 (de) | 1992-12-28 | 2005-11-03 | Baylink, David Jeston, Redlands | Methode zur messung der knochenresorption |
| DE59406512D1 (de) | 1993-07-28 | 1998-08-27 | Boehringer Mannheim Gmbh | Immunoassay zum nachweis von kollagen typ i oder kollagenfragmenten davon |
| DK104093D0 (da) | 1993-09-17 | 1993-09-17 | Osteometer A S | Fremgangsmaade til bestemmelse af collagen-fragmenter i legemsvaesker, test-kit og midler til udoevelse af fremgangsmaaden og anvendelse af fremgangsmaaden til diagnosticering af lidelser associeret til collagen-metabolismen |
| GB9506050D0 (en) * | 1995-03-24 | 1995-05-10 | Osteometer A S | Assaying collagen fragments in body fluids |
| JPH08100000A (ja) | 1994-09-30 | 1996-04-16 | Morinaga & Co Ltd | ヒトiv型コラーゲンに対する抗体及びその利用 |
| ES2154739T3 (es) | 1994-10-17 | 2001-04-16 | Osteometer Biotech As | Estimacion del modelo de fragmentacion del colageno en fluidos corporales y el diagnostico de trastornos asociados con el metabolismo del colageno. |
| US5763272A (en) | 1994-12-23 | 1998-06-09 | Boehringer Mannheim Gmbh | Hybridoma for producing antibody for collagen I |
| DE59505585D1 (de) | 1994-12-23 | 1999-05-12 | Roche Diagnostics Gmbh | Antigene und Antikörper zum Nachweis von Kollagen I |
| US5750647A (en) | 1995-05-19 | 1998-05-12 | Washington Research Foundation | Synthetic peptide analogs of NTx |
| JPH0921803A (ja) * | 1995-07-07 | 1997-01-21 | Teijin Ltd | 2型コラーゲンテロペプチドの測定方法 |
| US6107047A (en) * | 1996-03-21 | 2000-08-22 | Osteometer Biotech A/S | Assaying protein fragments in body fluids |
| GB9617616D0 (en) * | 1996-08-22 | 1996-10-02 | Osteometer Biotech As | Assaying protein fragments in body fluids |
| JP3446493B2 (ja) | 1996-09-13 | 2003-09-16 | トヨタ自動車株式会社 | エキゾーストマニホルド |
| EP0829724A1 (en) * | 1996-09-17 | 1998-03-18 | Nederlandse Organisatie Voor Toegepast-Natuurwetenschappelijk Onderzoek Tno | Assay for detecting collagen degradation |
| DE69705423T2 (de) * | 1996-12-09 | 2002-05-16 | Osteometer Biotech As Herlev | Sandwichtest zum nachweis von kollagenfragmenten |
| GB9702252D0 (en) * | 1997-02-06 | 1997-03-26 | Univ Sheffield Medical The Sch | Collagen assay |
-
1997
- 1997-12-05 DE DE69705423T patent/DE69705423T2/de not_active Expired - Lifetime
- 1997-12-05 ES ES97953745T patent/ES2160985T3/es not_active Expired - Lifetime
- 1997-12-05 WO PCT/EP1997/006803 patent/WO1998026286A2/en not_active Ceased
- 1997-12-05 AT AT97953745T patent/ATE202632T1/de not_active IP Right Cessation
- 1997-12-05 JP JP52618698A patent/JP3913787B2/ja not_active Expired - Fee Related
- 1997-12-05 US US09/319,539 patent/US6660481B2/en not_active Expired - Lifetime
- 1997-12-05 EP EP97953745A patent/EP0944833B1/en not_active Expired - Lifetime
- 1997-12-05 AU AU57542/98A patent/AU5754298A/en not_active Abandoned
-
2003
- 2003-12-09 US US10/730,070 patent/US7195883B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| EP0944833B1 (en) | 2001-06-27 |
| WO1998026286A2 (en) | 1998-06-18 |
| US7195883B2 (en) | 2007-03-27 |
| US6660481B2 (en) | 2003-12-09 |
| WO1998026286A3 (en) | 1998-08-13 |
| EP0944833A2 (en) | 1999-09-29 |
| ES2160985T3 (es) | 2001-11-16 |
| AU5754298A (en) | 1998-07-03 |
| ATE202632T1 (de) | 2001-07-15 |
| US20030148272A1 (en) | 2003-08-07 |
| DE69705423T2 (de) | 2002-05-16 |
| US20040224375A1 (en) | 2004-11-11 |
| JP2001506000A (ja) | 2001-05-08 |
| DE69705423D1 (de) | 2001-08-02 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5912131A (en) | Detection of type 1 collagen degradation in vivo | |
| EP0742902B1 (en) | A method of assaying collagen fragments in body fluids, a test kit and means for carrying out the method and use of the method to diagnose the presence of disorders associated with the metabolism of collagen | |
| JP3913787B2 (ja) | I型コラーゲン断片のサンドウイッチ測定法 | |
| US6323314B1 (en) | Method of assaying collagen fragments in body fluids, a test KT and means for carrying out the same | |
| JPH08505149A (ja) | 骨再吸収検定法 | |
| US6210902B1 (en) | Estimation of the fragmentation pattern of collagen in body fluids and the diagnosis of disorders associated with the metabolism of collagen | |
| US6300083B1 (en) | Assaying D-amino acids in body fluids | |
| WO1999006840A1 (en) | Collagen-peptide assay method | |
| US6117646A (en) | Assaying protein fragments in body fluids | |
| US6372442B1 (en) | Method of characterizing the degradation of type II collagen | |
| US6107047A (en) | Assaying protein fragments in body fluids | |
| US6420125B1 (en) | Assaying fragments of collagen in body fluids | |
| US20090042220A1 (en) | Method for monitoring collagen type II degradation in cartilage | |
| KR100460292B1 (ko) | 체액중의단백질파편검정 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| RD02 | Notification of acceptance of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7422 Effective date: 20040402 |
|
| RD04 | Notification of resignation of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7424 Effective date: 20040426 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20041029 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20041029 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20051018 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20060118 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20060306 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20060418 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20060912 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20061114 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20070116 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20070201 |
|
| R150 | Certificate of patent or registration of utility model |
Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20100209 Year of fee payment: 3 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20110209 Year of fee payment: 4 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20110209 Year of fee payment: 4 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20120209 Year of fee payment: 5 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20130209 Year of fee payment: 6 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20140209 Year of fee payment: 7 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| LAPS | Cancellation because of no payment of annual fees |