TWI411441B - 血管收縮素轉化酶抑制性肽類 - Google Patents
血管收縮素轉化酶抑制性肽類 Download PDFInfo
- Publication number
- TWI411441B TWI411441B TW100111621A TW100111621A TWI411441B TW I411441 B TWI411441 B TW I411441B TW 100111621 A TW100111621 A TW 100111621A TW 100111621 A TW100111621 A TW 100111621A TW I411441 B TWI411441 B TW I411441B
- Authority
- TW
- Taiwan
- Prior art keywords
- peptide
- tyr
- tripeptide
- inhibitory activity
- val
- Prior art date
Links
- 101710178392 Angiotensin-converting enzyme inhibitory peptide Proteins 0.000 title 1
- 235000003434 Sesamum indicum Nutrition 0.000 claims abstract description 14
- BZWUSZGQOILYEU-STECZYCISA-N Val-Ile-Tyr Chemical compound CC(C)[C@H](N)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 BZWUSZGQOILYEU-STECZYCISA-N 0.000 claims abstract description 11
- 230000029087 digestion Effects 0.000 claims abstract description 10
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 5
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 75
- 239000000203 mixture Substances 0.000 claims description 25
- 240000007594 Oryza sativa Species 0.000 claims description 14
- 235000007164 Oryza sativa Nutrition 0.000 claims description 14
- 102000004169 proteins and genes Human genes 0.000 claims description 14
- 108090000623 proteins and genes Proteins 0.000 claims description 14
- 244000075850 Avena orientalis Species 0.000 claims description 13
- 235000007319 Avena orientalis Nutrition 0.000 claims description 13
- 244000000231 Sesamum indicum Species 0.000 claims description 13
- 235000009566 rice Nutrition 0.000 claims description 13
- 240000005979 Hordeum vulgare Species 0.000 claims description 7
- 235000007340 Hordeum vulgare Nutrition 0.000 claims description 7
- 239000005541 ACE inhibitor Substances 0.000 claims description 6
- 244000046052 Phaseolus vulgaris Species 0.000 claims description 6
- 229940044094 angiotensin-converting-enzyme inhibitor Drugs 0.000 claims description 6
- 101710129690 Angiotensin-converting enzyme inhibitor Proteins 0.000 claims description 5
- 101710086378 Bradykinin-potentiating and C-type natriuretic peptides Proteins 0.000 claims description 5
- 244000068988 Glycine max Species 0.000 claims description 5
- 235000010469 Glycine max Nutrition 0.000 claims description 5
- 240000004922 Vigna radiata Species 0.000 claims description 5
- 239000002220 antihypertensive agent Substances 0.000 claims description 5
- 235000021307 Triticum Nutrition 0.000 claims description 4
- 240000006677 Vicia faba Species 0.000 claims description 4
- 235000010749 Vicia faba Nutrition 0.000 claims description 4
- 235000010721 Vigna radiata var radiata Nutrition 0.000 claims description 4
- 235000011469 Vigna radiata var sublobata Nutrition 0.000 claims description 4
- 230000037406 food intake Effects 0.000 claims description 4
- 108091005804 Peptidases Proteins 0.000 claims description 3
- 239000004365 Protease Substances 0.000 claims description 3
- 235000002098 Vicia faba var. major Nutrition 0.000 claims description 3
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 claims description 3
- 235000002017 Zea mays subsp mays Nutrition 0.000 claims description 3
- 239000004480 active ingredient Substances 0.000 claims description 3
- 235000005822 corn Nutrition 0.000 claims description 3
- 244000098338 Triticum aestivum Species 0.000 claims description 2
- 235000021332 kidney beans Nutrition 0.000 claims description 2
- 239000000463 material Substances 0.000 claims description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- 240000008042 Zea mays Species 0.000 claims 1
- 108090000882 Peptidyl-Dipeptidase A Proteins 0.000 abstract description 49
- UUUHXMGGBIUAPW-UHFFFAOYSA-N 1-[1-[2-[[5-amino-2-[[1-[5-(diaminomethylideneamino)-2-[[1-[3-(1h-indol-3-yl)-2-[(5-oxopyrrolidine-2-carbonyl)amino]propanoyl]pyrrolidine-2-carbonyl]amino]pentanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-methylpentanoyl]pyrrolidine-2-carbon Chemical compound C1CCC(C(=O)N2C(CCC2)C(O)=O)N1C(=O)C(C(C)CC)NC(=O)C(CCC(N)=O)NC(=O)C1CCCN1C(=O)C(CCCN=C(N)N)NC(=O)C1CCCN1C(=O)C(CC=1C2=CC=CC=C2NC=1)NC(=O)C1CCC(=O)N1 UUUHXMGGBIUAPW-UHFFFAOYSA-N 0.000 abstract description 48
- 230000002401 inhibitory effect Effects 0.000 abstract description 41
- MSFITIBEMPWCBD-ULQDDVLXSA-N Leu-Val-Tyr Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 MSFITIBEMPWCBD-ULQDDVLXSA-N 0.000 abstract description 19
- 108090001109 Thermolysin Proteins 0.000 abstract description 16
- IRMLZWSRWSGTOP-CIUDSAMLSA-N Leu-Ser-Ala Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(O)=O IRMLZWSRWSGTOP-CIUDSAMLSA-N 0.000 abstract description 7
- 230000001077 hypotensive effect Effects 0.000 abstract description 4
- 102000038379 digestive enzymes Human genes 0.000 abstract description 3
- 108091007734 digestive enzymes Proteins 0.000 abstract description 3
- 238000001727 in vivo Methods 0.000 abstract description 3
- 241001465754 Metazoa Species 0.000 abstract description 2
- 238000002474 experimental method Methods 0.000 abstract description 2
- 102100030988 Angiotensin-converting enzyme Human genes 0.000 abstract 4
- 241000207961 Sesamum Species 0.000 abstract 1
- 102000004270 Peptidyl-Dipeptidase A Human genes 0.000 description 48
- 238000000034 method Methods 0.000 description 21
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 21
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 18
- 239000000047 product Substances 0.000 description 18
- 102000004196 processed proteins & peptides Human genes 0.000 description 17
- 239000000843 powder Substances 0.000 description 16
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 15
- 235000013305 food Nutrition 0.000 description 15
- 239000007788 liquid Substances 0.000 description 14
- 235000018102 proteins Nutrition 0.000 description 13
- 238000004128 high performance liquid chromatography Methods 0.000 description 12
- VLKZOEOYAKHREP-UHFFFAOYSA-N n-Hexane Chemical compound CCCCCC VLKZOEOYAKHREP-UHFFFAOYSA-N 0.000 description 12
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 11
- 239000000872 buffer Substances 0.000 description 11
- 150000001413 amino acids Chemical class 0.000 description 10
- 238000006243 chemical reaction Methods 0.000 description 10
- 239000011347 resin Substances 0.000 description 10
- 229920005989 resin Polymers 0.000 description 10
- 238000001514 detection method Methods 0.000 description 9
- 238000003786 synthesis reaction Methods 0.000 description 9
- 206010020772 Hypertension Diseases 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 8
- 230000036772 blood pressure Effects 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 235000007558 Avena sp Nutrition 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 239000000706 filtrate Substances 0.000 description 7
- 239000012071 phase Substances 0.000 description 7
- 239000012264 purified product Substances 0.000 description 7
- 235000013361 beverage Nutrition 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 238000004519 manufacturing process Methods 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 239000011148 porous material Substances 0.000 description 6
- 238000002360 preparation method Methods 0.000 description 6
- 239000007787 solid Substances 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 239000008194 pharmaceutical composition Substances 0.000 description 5
- 239000002904 solvent Substances 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 4
- 230000004531 blood pressure lowering effect Effects 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 238000004440 column chromatography Methods 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 239000003480 eluent Substances 0.000 description 4
- 238000002523 gelfiltration Methods 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 238000004885 tandem mass spectrometry Methods 0.000 description 4
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 3
- 101000984728 Chiropsoides quadrigatus Angiotensin-converting enzyme inhibitory peptide Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 3
- 241000700159 Rattus Species 0.000 description 3
- 241000209140 Triticum Species 0.000 description 3
- 241000209149 Zea Species 0.000 description 3
- 230000004913 activation Effects 0.000 description 3
- 150000003862 amino acid derivatives Chemical class 0.000 description 3
- 238000011088 calibration curve Methods 0.000 description 3
- 239000000284 extract Substances 0.000 description 3
- 238000010438 heat treatment Methods 0.000 description 3
- 230000001631 hypertensive effect Effects 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 239000003456 ion exchange resin Substances 0.000 description 3
- 229920003303 ion-exchange polymer Polymers 0.000 description 3
- 239000002952 polymeric resin Substances 0.000 description 3
- 239000011541 reaction mixture Substances 0.000 description 3
- 238000004007 reversed phase HPLC Methods 0.000 description 3
- 239000007858 starting material Substances 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- 229920003002 synthetic resin Polymers 0.000 description 3
- 235000013616 tea Nutrition 0.000 description 3
- CNBUSIJNWNXLQQ-NSHDSACASA-N (2s)-3-(4-hydroxyphenyl)-2-[(2-methylpropan-2-yl)oxycarbonylamino]propanoic acid Chemical compound CC(C)(C)OC(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 CNBUSIJNWNXLQQ-NSHDSACASA-N 0.000 description 2
- CUKWUWBLQQDQAC-VEQWQPCFSA-N (3s)-3-amino-4-[[(2s)-1-[[(2s)-1-[[(2s)-1-[[(2s,3s)-1-[[(2s)-1-[(2s)-2-[[(1s)-1-carboxyethyl]carbamoyl]pyrrolidin-1-yl]-3-(1h-imidazol-5-yl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-methyl-1-ox Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C1=CC=C(O)C=C1 CUKWUWBLQQDQAC-VEQWQPCFSA-N 0.000 description 2
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 2
- 102400000344 Angiotensin-1 Human genes 0.000 description 2
- 101800000734 Angiotensin-1 Proteins 0.000 description 2
- 102400000345 Angiotensin-2 Human genes 0.000 description 2
- 101800000733 Angiotensin-2 Proteins 0.000 description 2
- 102000011632 Caseins Human genes 0.000 description 2
- 108010076119 Caseins Proteins 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- OAKJQQAXSVQMHS-UHFFFAOYSA-N Hydrazine Chemical compound NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 2
- MDXGYYOJGPFFJL-QMMMGPOBSA-N N(alpha)-t-butoxycarbonyl-L-leucine Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)OC(C)(C)C MDXGYYOJGPFFJL-QMMMGPOBSA-N 0.000 description 2
- 108090000284 Pepsin A Proteins 0.000 description 2
- 102000057297 Pepsin A Human genes 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- ORWYRWWVDCYOMK-HBZPZAIKSA-N angiotensin I Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC(C)C)C(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@@H](N)CC(O)=O)C(C)C)C1=CC=C(O)C=C1 ORWYRWWVDCYOMK-HBZPZAIKSA-N 0.000 description 2
- 229950006323 angiotensin ii Drugs 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 235000013339 cereals Nutrition 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 235000011389 fruit/vegetable juice Nutrition 0.000 description 2
- 210000001035 gastrointestinal tract Anatomy 0.000 description 2
- 239000008187 granular material Substances 0.000 description 2
- 235000013402 health food Nutrition 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 239000004615 ingredient Substances 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 235000019645 odor Nutrition 0.000 description 2
- IWDCLRJOBJJRNH-UHFFFAOYSA-N p-cresol Chemical compound CC1=CC=C(O)C=C1 IWDCLRJOBJJRNH-UHFFFAOYSA-N 0.000 description 2
- 229940111202 pepsin Drugs 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000003826 tablet Substances 0.000 description 2
- 238000010998 test method Methods 0.000 description 2
- 238000003325 tomography Methods 0.000 description 2
- PUUABEGDHGDROR-RYUDHWBXSA-N (2s)-4-methyl-2-[[(2s)-3-methyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]butanoyl]amino]pentanoic acid Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](C(C)C)NC(=O)OC(C)(C)C PUUABEGDHGDROR-RYUDHWBXSA-N 0.000 description 1
- QJCNLJWUIOIMMF-YUMQZZPRSA-N (2s,3s)-3-methyl-2-[(2-methylpropan-2-yl)oxycarbonylamino]pentanoic acid Chemical compound CC[C@H](C)[C@@H](C(O)=O)NC(=O)OC(C)(C)C QJCNLJWUIOIMMF-YUMQZZPRSA-N 0.000 description 1
- DIIIISSCIXVANO-UHFFFAOYSA-N 1,2-Dimethylhydrazine Chemical compound CNNC DIIIISSCIXVANO-UHFFFAOYSA-N 0.000 description 1
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- -1 ACE Proline derivatives Chemical class 0.000 description 1
- 241000238876 Acari Species 0.000 description 1
- 102000004881 Angiotensinogen Human genes 0.000 description 1
- 108090001067 Angiotensinogen Proteins 0.000 description 1
- 108010064733 Angiotensins Proteins 0.000 description 1
- 102000015427 Angiotensins Human genes 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 101800004538 Bradykinin Proteins 0.000 description 1
- 102400000967 Bradykinin Human genes 0.000 description 1
- 241000238366 Cephalopoda Species 0.000 description 1
- 206010008111 Cerebral haemorrhage Diseases 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 102000029816 Collagenase Human genes 0.000 description 1
- 108060005980 Collagenase Proteins 0.000 description 1
- 235000019750 Crude protein Nutrition 0.000 description 1
- 108010082495 Dietary Plant Proteins Proteins 0.000 description 1
- 108010061435 Enalapril Proteins 0.000 description 1
- KRHYYFGTRYWZRS-UHFFFAOYSA-N Fluorane Chemical compound F KRHYYFGTRYWZRS-UHFFFAOYSA-N 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- QXZGBUJJYSLZLT-UHFFFAOYSA-N H-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-OH Natural products NC(N)=NCCCC(N)C(=O)N1CCCC1C(=O)N1C(C(=O)NCC(=O)NC(CC=2C=CC=CC=2)C(=O)NC(CO)C(=O)N2C(CCC2)C(=O)NC(CC=2C=CC=CC=2)C(=O)NC(CCCN=C(N)N)C(O)=O)CCC1 QXZGBUJJYSLZLT-UHFFFAOYSA-N 0.000 description 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 208000032843 Hemorrhage Diseases 0.000 description 1
- MMFKFJORZBJVNF-UWVGGRQHSA-N His-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@@H](N)CC1=CN=CN1 MMFKFJORZBJVNF-UWVGGRQHSA-N 0.000 description 1
- QSXSHZIRKTUXNG-STECZYCISA-N Ile-Val-Tyr Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CC1=CC=C(O)C=C1 QSXSHZIRKTUXNG-STECZYCISA-N 0.000 description 1
- 108060005987 Kallikrein Proteins 0.000 description 1
- 102000001399 Kallikrein Human genes 0.000 description 1
- 108010077861 Kininogens Proteins 0.000 description 1
- 102000010631 Kininogens Human genes 0.000 description 1
- 108010093008 Kinins Proteins 0.000 description 1
- 102000002397 Kinins Human genes 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 241001399426 Myas Species 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 108010064851 Plant Proteins Proteins 0.000 description 1
- 108090000783 Renin Proteins 0.000 description 1
- 102100028255 Renin Human genes 0.000 description 1
- 241001125046 Sardina pilchardus Species 0.000 description 1
- 241000893841 Schlechterella abyssinica Species 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 244000269722 Thea sinensis Species 0.000 description 1
- 244000098345 Triticum durum Species 0.000 description 1
- 244000191914 Triticum persicum Species 0.000 description 1
- 240000002805 Triticum turgidum Species 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- GXBMIBRIOWHPDT-UHFFFAOYSA-N Vasopressin Natural products N1C(=O)C(CC=2C=C(O)C=CC=2)NC(=O)C(N)CSSCC(C(=O)N2C(CCC2)C(=O)NC(CCCN=C(N)N)C(=O)NCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC(=O)C1CC1=CC=CC=C1 GXBMIBRIOWHPDT-UHFFFAOYSA-N 0.000 description 1
- 108010004977 Vasopressins Proteins 0.000 description 1
- 102000002852 Vasopressins Human genes 0.000 description 1
- 235000006582 Vigna radiata Nutrition 0.000 description 1
- 229920002494 Zein Polymers 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 125000003277 amino group Chemical group 0.000 description 1
- 229940030600 antihypertensive agent Drugs 0.000 description 1
- 229940124572 antihypotensive agent Drugs 0.000 description 1
- 210000000576 arachnoid Anatomy 0.000 description 1
- KBZOIRJILGZLEJ-LGYYRGKSSA-N argipressin Chemical compound C([C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSC[C@@H](C(N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N1)=O)N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(N)=O)C1=CC=CC=C1 KBZOIRJILGZLEJ-LGYYRGKSSA-N 0.000 description 1
- 235000015895 biscuits Nutrition 0.000 description 1
- QXZGBUJJYSLZLT-FDISYFBBSA-N bradykinin Chemical compound NC(=N)NCCC[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(=O)NCC(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CO)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)CCC1 QXZGBUJJYSLZLT-FDISYFBBSA-N 0.000 description 1
- 235000010633 broth Nutrition 0.000 description 1
- FAKRSMQSSFJEIM-RQJHMYQMSA-N captopril Chemical compound SC[C@@H](C)C(=O)N1CCC[C@H]1C(O)=O FAKRSMQSSFJEIM-RQJHMYQMSA-N 0.000 description 1
- 229960000830 captopril Drugs 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 206010008118 cerebral infarction Diseases 0.000 description 1
- 208000026106 cerebrovascular disease Diseases 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 235000020965 cold beverage Nutrition 0.000 description 1
- 229960002424 collagenase Drugs 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 235000008504 concentrate Nutrition 0.000 description 1
- 235000013409 condiments Nutrition 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 230000008602 contraction Effects 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 235000015872 dietary supplement Nutrition 0.000 description 1
- 230000001079 digestive effect Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- GBXSMTUPTTWBMN-XIRDDKMYSA-N enalapril Chemical compound C([C@@H](C(=O)OCC)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(O)=O)CC1=CC=CC=C1 GBXSMTUPTTWBMN-XIRDDKMYSA-N 0.000 description 1
- 229960000873 enalapril Drugs 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 230000005284 excitation Effects 0.000 description 1
- 235000013312 flour Nutrition 0.000 description 1
- 239000010200 folin Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 108010025306 histidylleucine Proteins 0.000 description 1
- 229910000040 hydrogen fluoride Inorganic materials 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 238000001361 intraarterial administration Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 108010060857 isoleucyl-valyl-tyrosine Proteins 0.000 description 1
- 235000015110 jellies Nutrition 0.000 description 1
- 235000021056 liquid food Nutrition 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 210000002464 muscle smooth vascular Anatomy 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 239000005445 natural material Substances 0.000 description 1
- 229920002113 octoxynol Polymers 0.000 description 1
- 229940126701 oral medication Drugs 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 235000021118 plant-derived protein Nutrition 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000002203 pretreatment Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000013777 protein digestion Effects 0.000 description 1
- 239000008213 purified water Substances 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 230000029865 regulation of blood pressure Effects 0.000 description 1
- 230000036454 renin-angiotensin system Effects 0.000 description 1
- 235000019512 sardine Nutrition 0.000 description 1
- 238000005204 segregation Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 235000021055 solid food Nutrition 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 239000008174 sterile solution Substances 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 230000035488 systolic blood pressure Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 239000005526 vasoconstrictor agent Substances 0.000 description 1
- 229960003726 vasopressin Drugs 0.000 description 1
- 239000005019 zein Substances 0.000 description 1
- 229940093612 zein Drugs 0.000 description 1
- 235000021246 κ-casein Nutrition 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
- C07K5/0808—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing 2 to 4 carbon atoms, e.g. Val, Ile, Leu
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/04—Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
- A61K38/06—Tripeptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/55—Protease inhibitors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/12—Antihypertensives
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Epidemiology (AREA)
- Cardiology (AREA)
- Heart & Thoracic Surgery (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2003074488 | 2003-03-18 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| TW201125574A TW201125574A (en) | 2011-08-01 |
| TWI411441B true TWI411441B (zh) | 2013-10-11 |
Family
ID=33027809
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW100111621A TWI411441B (zh) | 2003-03-18 | 2004-03-15 | 血管收縮素轉化酶抑制性肽類 |
| TW097129374A TWI344371B (en) | 2003-03-18 | 2004-03-15 | Angiotensin-converting enzyme inhibitory peptides |
| TW093106867A TWI328457B (en) | 2003-03-18 | 2004-03-15 | Angiotensin-converting enzyme inhibitory peptides |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| TW097129374A TWI344371B (en) | 2003-03-18 | 2004-03-15 | Angiotensin-converting enzyme inhibitory peptides |
| TW093106867A TWI328457B (en) | 2003-03-18 | 2004-03-15 | Angiotensin-converting enzyme inhibitory peptides |
Country Status (14)
| Country | Link |
|---|---|
| US (2) | US7833985B2 (enExample) |
| EP (3) | EP2145630B1 (enExample) |
| JP (3) | JP4283848B2 (enExample) |
| KR (3) | KR101078628B1 (enExample) |
| CN (1) | CN100402089C (enExample) |
| AU (3) | AU2004222435B2 (enExample) |
| CA (3) | CA2743539C (enExample) |
| CY (1) | CY1114072T1 (enExample) |
| DK (1) | DK1605969T3 (enExample) |
| ES (3) | ES2400561T3 (enExample) |
| PL (3) | PL1938832T3 (enExample) |
| PT (1) | PT1605969E (enExample) |
| TW (3) | TWI411441B (enExample) |
| WO (1) | WO2004082709A1 (enExample) |
Families Citing this family (41)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP4046708B2 (ja) * | 2004-06-04 | 2008-02-13 | 明治製菓株式会社 | ３−アルケニルセフェム化合物の製造方法 |
| JP2006219420A (ja) * | 2005-02-10 | 2006-08-24 | Nagase Chemtex Corp | 抗高血圧剤 |
| ATE497704T1 (de) * | 2005-04-28 | 2011-02-15 | Unilever Nv | Gesundheitsfördernde peptide und sie enthaltende zusammensetzungen |
| EP1874129A1 (en) * | 2005-04-28 | 2008-01-09 | Unilever PLC | Peptides having an ace inhibiting effect |
| BRPI0611469A2 (pt) * | 2005-04-28 | 2010-09-08 | Unilever Nv | usos do tripeptìdeo itp e produto alimentìcio |
| US20090143311A1 (en) * | 2005-04-28 | 2009-06-04 | Luppo Edens | Compositions comprising tripeptides inhibiting ace |
| EP1726659B1 (en) * | 2005-05-24 | 2009-12-30 | Chr. Hansen A/S | Isolated dipeptides with ACE inhibitor effect |
| JP4994093B2 (ja) * | 2006-04-13 | 2012-08-08 | ロート製薬株式会社 | 育毛剤 |
| CN100456948C (zh) * | 2006-06-30 | 2009-02-04 | 北京三友汇智生物技术有限公司 | 一种燕麦肽及其提取方法 |
| KR100787949B1 (ko) * | 2007-08-29 | 2007-12-24 | 한양대학교 산학협력단 | 대두 발효 조성물의 제조방법 및 이 조성물로부터 유래된펩타이드 |
| JP2009073765A (ja) * | 2007-09-20 | 2009-04-09 | Nitsukoku Seifun Kk | アンジオテンシン変換酵素（ａｃｅ）阻害剤組成物及びその製造方法 |
| JP2010163400A (ja) | 2009-01-19 | 2010-07-29 | Kikkoman Corp | 新規アンジオテンシン変換酵素阻害ペプチド |
| CN101618207B (zh) * | 2009-06-17 | 2011-08-03 | 中国科学院大连化学物理研究所 | 多肽在制备ace抑制剂及降血压药物中的应用 |
| US20120157395A1 (en) * | 2009-07-13 | 2012-06-21 | Masahisa Ibuki | Anti-inflammatory agent for oral application, and anti-inflammatory peptide for oral application |
| CN101696233B (zh) * | 2009-10-29 | 2012-02-01 | 吉林大学 | 蛋清蛋白血管紧张素转化酶抑制肽及其制备 |
| JP5654290B2 (ja) * | 2010-08-27 | 2015-01-14 | ユニチカ株式会社 | アンジオテンシン変換酵素阻害ペプチド及びその製造方法。 |
| CN102399261B (zh) * | 2010-09-07 | 2014-06-25 | 任发政 | 具有血管紧张素转化酶c-端选择性抑制活性的三肽及其应用和组合物 |
| CN102475884B (zh) * | 2010-11-29 | 2013-08-14 | 中国科学院大连化学物理研究所 | 四个多肽在制备ace抑制剂及降血压药物中的应用 |
| CN102276690B (zh) * | 2011-08-05 | 2013-03-20 | 成都中医药大学 | 降血压功能性多肽及其用途 |
| JP6296722B2 (ja) * | 2012-07-31 | 2018-03-20 | サンスター株式会社 | 米糠酵素処理組成物 |
| KR101481416B1 (ko) * | 2012-10-17 | 2015-01-13 | 건국대학교 산학협력단 | 안지오텐신 전환 효소 저해 활성을 갖는 펩타이드 |
| JP2014141462A (ja) * | 2012-12-27 | 2014-08-07 | Raffinee International Co Ltd | ペプチド、並びに、アンジオテンシン変換酵素阻害剤、抗高血圧剤、及び飲食品 |
| AU2014225786B2 (en) | 2013-03-08 | 2017-10-12 | Axiom Foods, Inc. | Rice protein supplements |
| CN103172698B (zh) * | 2013-04-10 | 2015-02-18 | 华东理工大学 | 降血压多肽 |
| CN103242430B (zh) * | 2013-05-31 | 2014-10-08 | 南京中医药大学 | 血管紧张素转化酶抑制肽及其制备方法和应用 |
| CN103290086B (zh) * | 2013-06-25 | 2015-01-14 | 广州合诚实业有限公司 | 具有ace抑制活性的绿豆蛋白肽及其制备方法与应用 |
| CN104558109B (zh) * | 2013-10-21 | 2018-06-08 | 中国科学院大连化学物理研究所 | 源于油菜花粉的具有ace抑制活性的多肽化合物及应用 |
| CN104558110B (zh) * | 2013-10-21 | 2018-06-08 | 中国科学院大连化学物理研究所 | 具有ace抑制活性的多肽及其在降血压药物中的应用 |
| CN107417768B (zh) * | 2014-11-25 | 2021-01-29 | 烟台市华昕生物医药科技有限公司 | 一种从荠莱中分离获得的降血压多肽 |
| CN109563129B (zh) * | 2016-06-16 | 2022-04-01 | 太阳星光齿磨公司 | 新型三肽 |
| CN106188227B (zh) * | 2016-07-07 | 2019-09-24 | 华东理工大学 | 降血压肽和降血压蛋白质及其应用 |
| CN110868870A (zh) | 2017-05-12 | 2020-03-06 | 艾斯姆食品公司 | 大米产物及制备它们的系统和方法 |
| WO2019006952A1 (zh) * | 2017-07-07 | 2019-01-10 | 广州世优生物科技有限公司 | 含环非极性二肽在制备降血压药物或保健品中的应用 |
| CN110498833B (zh) * | 2019-08-30 | 2021-01-15 | 华南理工大学 | 一种具有ace抑制作用的三肽及其应用 |
| EP4072315B1 (en) * | 2019-12-09 | 2026-07-01 | Société des Produits Nestlé S.A. | PASTE FOR PREPARING A DRINK |
| JP7391738B2 (ja) * | 2020-03-19 | 2023-12-05 | Ｋｉｓｃｏ株式会社 | ペプチド、及び苦味付与剤 |
| CN111548387B (zh) * | 2020-03-31 | 2020-12-18 | 华南农业大学 | 一种具有降血压功效的寡肽及其制备方法与应用 |
| CN111471086B (zh) * | 2020-04-16 | 2023-01-24 | 河南省农业科学院 | 芝麻多肽及其制备方法和应用 |
| CN111825754B (zh) * | 2020-07-16 | 2022-02-11 | 河南省农业科学院 | 一种从芝麻蛋白中获得的具有降血压与降血糖活性的多肽 |
| WO2022168413A1 (ja) * | 2021-02-04 | 2022-08-11 | ユーハ味覚糖株式会社 | デプレスタチン含有組成物の製造方法 |
| CN120904281B (zh) * | 2025-08-05 | 2025-12-23 | 北京雯茵生物科技有限公司 | 生物活性肽及其在治疗心脑血管疾病中的应用 |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1018341A1 (en) * | 1997-09-26 | 2000-07-12 | Calpis Co., Ltd. | Antistress agents and functional foods |
| EP1092724A2 (en) * | 1999-10-15 | 2001-04-18 | The Nippon Synthetic Chemical Industry Co., Ltd. | Angiotensin converting enzyme inhibitor |
| WO2001068115A1 (en) * | 2000-03-13 | 2001-09-20 | Monsanto Technology Llc | Process for producing peptide sequences possessing anti-hypertension activity |
| WO2001081368A2 (en) * | 2000-04-21 | 2001-11-01 | Monsanto Technology Llc | Blood-pressure reducing polypeptides containing vpp derived from microorganisms |
Family Cites Families (31)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS52148631A (en) | 1976-06-01 | 1977-12-10 | Kitazato Daigaku Yakurigakubu | Enzym obstruction agent |
| DE3112394A1 (de) * | 1980-07-22 | 1982-07-08 | Eltreva AG, 4147 Aesch | "einrichtung zur luftregulierung einer energiefassade" |
| JPS6023085B2 (ja) | 1981-12-23 | 1985-06-05 | 工業技術院長 | アンジオテンシン転換酵素阻害剤 |
| US5156840A (en) * | 1982-03-09 | 1992-10-20 | Cytogen Corporation | Amine-containing porphyrin derivatives |
| US4867973A (en) * | 1984-08-31 | 1989-09-19 | Cytogen Corporation | Antibody-therapeutic agent conjugates |
| JPS6023086B2 (ja) | 1982-09-04 | 1985-06-05 | 工業技術院長 | アンジオテンシン転換酵素阻害剤 |
| JPS6023086A (ja) | 1983-07-20 | 1985-02-05 | Canon Inc | リボンカセツト |
| JPS6023087A (ja) | 1983-07-20 | 1985-02-05 | Canon Inc | リボンカセツト |
| DE3485587D1 (de) * | 1983-08-16 | 1992-04-23 | Univ Georgia Res Found | Herstellung von aminocyclopropancarbonsaeuren und von peptiden. |
| JPS6136226A (ja) | 1984-07-28 | 1986-02-20 | Agency Of Ind Science & Technol | アンジオテンシン転換酵素阻害剤 |
| JPS6136227A (ja) | 1984-07-28 | 1986-02-20 | Agency Of Ind Science & Technol | アンジオテンシン転換酵素阻害剤 |
| JPS6286741A (ja) | 1985-10-11 | 1987-04-21 | Mitsubishi Electric Corp | パタ−ンの位置合わせずれ量評価方法 |
| JP2805032B2 (ja) | 1988-07-27 | 1998-09-30 | 工業技術院長 | アンジオテンシン変換酵素阻害剤 |
| JP2873318B2 (ja) | 1989-03-14 | 1999-03-24 | 工業技術院長 | 血圧降下剤 |
| JPH0311097A (ja) | 1989-06-07 | 1991-01-18 | Senmi Ekisu Kk | 新規ペプチド |
| JPH0623086B2 (ja) | 1989-07-19 | 1994-03-30 | 花王株式会社 | 洗浄剤組成物 |
| DE69124274T2 (de) * | 1990-02-27 | 1997-08-14 | Agency Ind Science Techn | Oligopeptide, sie enthaltende pharmazeutische und Futterzusammensetzung und Benützung von Oligopeptiden |
| JP3103363B2 (ja) * | 1990-03-30 | 2000-10-30 | 昭和産業株式会社 | 新規トリペプチド及び血圧降下剤 |
| JP3073762B2 (ja) | 1990-10-03 | 2000-08-07 | 日本合成化学工業株式会社 | アンギオテンシン変換酵素阻害剤含有組成物の製造方法 |
| JPH06136227A (ja) | 1992-10-22 | 1994-05-17 | Nippon Steel Chem Co Ltd | 熱可塑性樹脂組成物 |
| JP3357097B2 (ja) | 1992-10-27 | 2002-12-16 | 株式会社クラレ | 耐衝撃性メタクリル樹脂組成物 |
| JP2820868B2 (ja) | 1993-08-27 | 1998-11-05 | 日清食品株式会社 | アンジオテンシン変換酵素阻害蛋白分解物 |
| ES2170105T3 (es) * | 1993-10-04 | 2002-08-01 | Pasteur Institut | Compuestos que modifican la transmision serotoninergica; aplicaciones diagnosticas y terapeuticas. |
| US5558993A (en) * | 1994-06-17 | 1996-09-24 | The Regents Of The University Of California | Cloned Borrelia burgdorferi virulence protein |
| JP3135812B2 (ja) | 1995-03-01 | 2001-02-19 | 日清食品株式会社 | アンジオテンシン変換酵素阻害ペプチドおよびその製造方法 |
| JP3567012B2 (ja) | 1995-03-28 | 2004-09-15 | 雪印乳業株式会社 | 新規ペプチド及びその利用 |
| JP3028411B2 (ja) * | 1997-09-26 | 2000-04-04 | カルピス株式会社 | トリペプチド高生産性ラクトバチルス・ヘルベチカス乳酸菌 |
| CN1377276A (zh) * | 1999-08-09 | 2002-10-30 | 特里帕普股份公司 | 含有三肽的药用组合物 |
| FI113741B (fi) * | 1999-11-01 | 2004-06-15 | Valio Oy | Menetelmä verenpainetta alentavia peptidejä sisältävän tuotteen valmistamiseksi |
| CN1491278A (zh) * | 2001-02-07 | 2004-04-21 | ŵά�Ź�˾ | 脂酶变体 |
| JP4144696B2 (ja) | 2002-11-07 | 2008-09-03 | タイヨーエレック株式会社 | 遊技機 |
-
2004
- 2004-03-15 TW TW100111621A patent/TWI411441B/zh not_active IP Right Cessation
- 2004-03-15 TW TW097129374A patent/TWI344371B/zh not_active IP Right Cessation
- 2004-03-15 TW TW093106867A patent/TWI328457B/zh not_active IP Right Cessation
- 2004-03-17 US US10/549,176 patent/US7833985B2/en not_active Expired - Fee Related
- 2004-03-17 CN CNB2004800112694A patent/CN100402089C/zh not_active Expired - Lifetime
- 2004-03-17 JP JP2006507670A patent/JP4283848B2/ja not_active Expired - Lifetime
- 2004-03-17 CA CA2743539A patent/CA2743539C/en not_active Expired - Fee Related
- 2004-03-17 ES ES04721339T patent/ES2400561T3/es not_active Expired - Lifetime
- 2004-03-17 DK DK04721339.2T patent/DK1605969T3/da active
- 2004-03-17 ES ES08153738T patent/ES2400308T3/es not_active Expired - Lifetime
- 2004-03-17 PL PL08153738T patent/PL1938832T3/pl unknown
- 2004-03-17 AU AU2004222435A patent/AU2004222435B2/en not_active Ceased
- 2004-03-17 EP EP09172830A patent/EP2145630B1/en not_active Expired - Lifetime
- 2004-03-17 KR KR1020117000079A patent/KR101078628B1/ko not_active Expired - Fee Related
- 2004-03-17 EP EP04721339A patent/EP1605969B1/en not_active Expired - Lifetime
- 2004-03-17 EP EP08153738A patent/EP1938832B1/en not_active Expired - Lifetime
- 2004-03-17 PL PL09172830T patent/PL2145630T3/pl unknown
- 2004-03-17 CA CA2526891A patent/CA2526891C/en not_active Expired - Fee Related
- 2004-03-17 KR KR1020057017447A patent/KR101119449B1/ko not_active Expired - Fee Related
- 2004-03-17 CA CA2743313A patent/CA2743313C/en not_active Expired - Fee Related
- 2004-03-17 KR KR1020117000078A patent/KR101077801B1/ko not_active Expired - Fee Related
- 2004-03-17 WO PCT/JP2004/003588 patent/WO2004082709A1/en not_active Ceased
- 2004-03-17 PL PL04721339T patent/PL1605969T3/pl unknown
- 2004-03-17 PT PT47213392T patent/PT1605969E/pt unknown
- 2004-03-17 ES ES09172830T patent/ES2398788T3/es not_active Expired - Lifetime
-
2008
- 2008-12-01 JP JP2008306269A patent/JP4369986B2/ja not_active Expired - Lifetime
- 2008-12-01 JP JP2008306249A patent/JP4369985B2/ja not_active Expired - Lifetime
-
2009
- 2009-06-12 US US12/483,676 patent/US7943578B2/en not_active Expired - Fee Related
- 2009-11-12 AU AU2009236034A patent/AU2009236034B2/en not_active Ceased
- 2009-11-12 AU AU2009236033A patent/AU2009236033B2/en not_active Ceased
-
2013
- 2013-04-26 CY CY20131100344T patent/CY1114072T1/el unknown
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1018341A1 (en) * | 1997-09-26 | 2000-07-12 | Calpis Co., Ltd. | Antistress agents and functional foods |
| EP1092724A2 (en) * | 1999-10-15 | 2001-04-18 | The Nippon Synthetic Chemical Industry Co., Ltd. | Angiotensin converting enzyme inhibitor |
| WO2001068115A1 (en) * | 2000-03-13 | 2001-09-20 | Monsanto Technology Llc | Process for producing peptide sequences possessing anti-hypertension activity |
| WO2001081368A2 (en) * | 2000-04-21 | 2001-11-01 | Monsanto Technology Llc | Blood-pressure reducing polypeptides containing vpp derived from microorganisms |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| TWI344371B (en) | Angiotensin-converting enzyme inhibitory peptides | |
| US20060234942A1 (en) | Use of at least one $g(a)62 casein peptide with angiotensin i converting enzyme inhibiting activity for preparing medicines, food products and food complements | |
| JP5417405B2 (ja) | アンジオテンシン変換酵素阻害性降圧ペプチド組成物の製造方法 | |
| JPH04275298A (ja) | ぺプチド及びこれを有効成分とするアンジオテンシン変換酵素阻害剤 | |
| HK1084604B (en) | Angiotensin-converting enzyme inhibitory peptides |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MK4A | Expiration of patent term of an invention patent |