IL42594A - Cancer associated polypeptide antigen,its preparation,its detection and immunizing compositions containing it - Google Patents
Cancer associated polypeptide antigen,its preparation,its detection and immunizing compositions containing itInfo
- Publication number
- IL42594A IL42594A IL42594A IL4259473A IL42594A IL 42594 A IL42594 A IL 42594A IL 42594 A IL42594 A IL 42594A IL 4259473 A IL4259473 A IL 4259473A IL 42594 A IL42594 A IL 42594A
- Authority
- IL
- Israel
- Prior art keywords
- capa
- process according
- gel
- resulting
- fraction
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract 14
- 239000000427 antigen Substances 0.000 title claims abstract 13
- 102000036639 antigens Human genes 0.000 title claims abstract 13
- 108091007433 antigens Proteins 0.000 title claims abstract 13
- 229920001184 polypeptide Polymers 0.000 title claims abstract 13
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract 13
- 239000000203 mixture Substances 0.000 title claims abstract 12
- 206010028980 Neoplasm Diseases 0.000 title claims abstract 9
- 201000011510 cancer Diseases 0.000 title claims 5
- 238000002360 preparation method Methods 0.000 title abstract 2
- 238000001514 detection method Methods 0.000 title 1
- 230000003053 immunization Effects 0.000 title 1
- 239000000463 material Substances 0.000 claims abstract 14
- 239000007787 solid Substances 0.000 claims abstract 7
- 239000007864 aqueous solution Substances 0.000 claims abstract 6
- 239000002808 molecular sieve Substances 0.000 claims abstract 6
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 claims abstract 6
- 239000002253 acid Substances 0.000 claims abstract 4
- 238000004587 chromatography analysis Methods 0.000 claims abstract 4
- 238000001914 filtration Methods 0.000 claims abstract 4
- 239000007788 liquid Substances 0.000 claims abstract 3
- 239000011324 bead Substances 0.000 claims abstract 2
- 150000001875 compounds Chemical class 0.000 claims abstract 2
- 239000000284 extract Substances 0.000 claims abstract 2
- 238000005194 fractionation Methods 0.000 claims abstract 2
- 239000003960 organic solvent Substances 0.000 claims abstract 2
- 238000001556 precipitation Methods 0.000 claims abstract 2
- 238000000034 method Methods 0.000 claims 31
- 239000000499 gel Substances 0.000 claims 16
- 239000000839 emulsion Substances 0.000 claims 6
- 241001465754 Metazoa Species 0.000 claims 4
- 229920002401 polyacrylamide Polymers 0.000 claims 4
- 229920005654 Sephadex Polymers 0.000 claims 3
- 238000010521 absorption reaction Methods 0.000 claims 3
- 210000004027 cell Anatomy 0.000 claims 3
- 238000000227 grinding Methods 0.000 claims 3
- 150000002500 ions Chemical class 0.000 claims 3
- 239000000243 solution Substances 0.000 claims 3
- 229920001817 Agar Polymers 0.000 claims 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 claims 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims 2
- 241001494479 Pecora Species 0.000 claims 2
- 239000002671 adjuvant Substances 0.000 claims 2
- 239000008272 agar Substances 0.000 claims 2
- 239000011543 agarose gel Substances 0.000 claims 2
- 210000000601 blood cell Anatomy 0.000 claims 2
- 230000003247 decreasing effect Effects 0.000 claims 2
- 238000010828 elution Methods 0.000 claims 2
- 238000002523 gelfiltration Methods 0.000 claims 2
- 239000004816 latex Substances 0.000 claims 2
- 229920000126 latex Polymers 0.000 claims 2
- 238000004519 manufacturing process Methods 0.000 claims 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 claims 2
- 238000002156 mixing Methods 0.000 claims 2
- 230000007935 neutral effect Effects 0.000 claims 2
- 239000011236 particulate material Substances 0.000 claims 2
- 210000002966 serum Anatomy 0.000 claims 2
- GNFTZDOKVXKIBK-UHFFFAOYSA-N 3-(2-methoxyethoxy)benzohydrazide Chemical compound COCCOC1=CC=CC(C(=O)NN)=C1 GNFTZDOKVXKIBK-UHFFFAOYSA-N 0.000 claims 1
- LJGHYPLBDBRCRZ-UHFFFAOYSA-N 3-(3-aminophenyl)sulfonylaniline Chemical compound NC1=CC=CC(S(=O)(=O)C=2C=C(N)C=CC=2)=C1 LJGHYPLBDBRCRZ-UHFFFAOYSA-N 0.000 claims 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 claims 1
- 239000004475 Arginine Substances 0.000 claims 1
- 102000004190 Enzymes Human genes 0.000 claims 1
- 108090000790 Enzymes Proteins 0.000 claims 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims 1
- 239000004471 Glycine Substances 0.000 claims 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims 1
- 239000004472 Lysine Substances 0.000 claims 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims 1
- 241000283973 Oryctolagus cuniculus Species 0.000 claims 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims 1
- 229910000831 Steel Inorganic materials 0.000 claims 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims 1
- 239000004473 Threonine Substances 0.000 claims 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims 1
- 239000002535 acidifier Substances 0.000 claims 1
- 239000004480 active ingredient Substances 0.000 claims 1
- 235000004279 alanine Nutrition 0.000 claims 1
- 235000001014 amino acid Nutrition 0.000 claims 1
- 229940024606 amino acid Drugs 0.000 claims 1
- 150000001413 amino acids Chemical class 0.000 claims 1
- 210000000628 antibody-producing cell Anatomy 0.000 claims 1
- 239000006286 aqueous extract Substances 0.000 claims 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims 1
- 235000003704 aspartic acid Nutrition 0.000 claims 1
- 229910000278 bentonite Inorganic materials 0.000 claims 1
- 239000000440 bentonite Substances 0.000 claims 1
- SVPXDRXYRYOSEX-UHFFFAOYSA-N bentoquatam Chemical compound O.O=[Si]=O.O=[Al]O[Al]=O SVPXDRXYRYOSEX-UHFFFAOYSA-N 0.000 claims 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims 1
- 238000001574 biopsy Methods 0.000 claims 1
- 210000004369 blood Anatomy 0.000 claims 1
- 239000008280 blood Substances 0.000 claims 1
- 230000000536 complexating effect Effects 0.000 claims 1
- 235000018417 cysteine Nutrition 0.000 claims 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims 1
- 230000003297 denaturating effect Effects 0.000 claims 1
- 239000003937 drug carrier Substances 0.000 claims 1
- 235000019253 formic acid Nutrition 0.000 claims 1
- 230000008014 freezing Effects 0.000 claims 1
- 238000007710 freezing Methods 0.000 claims 1
- 235000013922 glutamic acid Nutrition 0.000 claims 1
- 239000004220 glutamic acid Substances 0.000 claims 1
- 238000010438 heat treatment Methods 0.000 claims 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims 1
- 238000000265 homogenisation Methods 0.000 claims 1
- 229940124452 immunizing agent Drugs 0.000 claims 1
- 239000012535 impurity Substances 0.000 claims 1
- 238000000338 in vitro Methods 0.000 claims 1
- 238000011534 incubation Methods 0.000 claims 1
- 230000005764 inhibitory process Effects 0.000 claims 1
- 230000003993 interaction Effects 0.000 claims 1
- 238000002955 isolation Methods 0.000 claims 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims 1
- 229960000310 isoleucine Drugs 0.000 claims 1
- 229930182817 methionine Natural products 0.000 claims 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims 1
- 210000002826 placenta Anatomy 0.000 claims 1
- 239000002244 precipitate Substances 0.000 claims 1
- 238000013207 serial dilution Methods 0.000 claims 1
- 239000002904 solvent Substances 0.000 claims 1
- 238000002798 spectrophotometry method Methods 0.000 claims 1
- 230000000087 stabilizing effect Effects 0.000 claims 1
- 239000010959 steel Substances 0.000 claims 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims 1
- 239000004474 valine Substances 0.000 claims 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims 1
- 230000000890 antigenic effect Effects 0.000 abstract 2
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
- G01N33/574—Immunoassay; Biospecific binding assay; Materials therefor for cancer
- G01N33/57484—Immunoassay; Biospecific binding assay; Materials therefor for cancer involving compounds serving as markers for tumor, cancer, neoplasia, e.g. cellular determinants, receptors, heat shock/stress proteins, A-protein, oligosaccharides, metabolites
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/0005—Vertebrate antigens
- A61K39/0011—Cancer antigens
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Immunology (AREA)
- Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Microbiology (AREA)
- Oncology (AREA)
- Molecular Biology (AREA)
- Urology & Nephrology (AREA)
- Mycology (AREA)
- Epidemiology (AREA)
- Hematology (AREA)
- Cell Biology (AREA)
- Biomedical Technology (AREA)
- Organic Chemistry (AREA)
- Biotechnology (AREA)
- Hospice & Palliative Care (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Food Science & Technology (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Biochemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Abstract
To obtain a tumour polypeptide antigen, initially material with tumour polypeptide antigenic activity is homogenised in a liquid at a temperature not exceeding 0 DEG C. The solids are removed from the mixture of liquid homogenate and solids directly or after treatment with an organic solvent in the cold. The solids are extracted with an alkaline aqueous solution. The extract is filtered through a filtration gel of the molecular sieve type in bead form which permits fractionation of compounds with a molecular weight in the range from 10,000 to 20 x 10<6>, the gel is eluted and the fraction with a molecular weight of 10 x 10<6> to 20 x 10<6> is obtained. The resulting fraction is purified by chromatography. The fraction having antigenic activity is obtained and subjected to isoelectric precipitation by adding acid until the solubility of the polypeptides reaches a minimum as a consequence of the presence of the polypeptide molecules in the form of zwitterions. Subsequently, the polypeptide antigen is further purified. The resulting tumour polypeptide antigen can be used for the preparation of antibodies which are monospecific for the polypeptide antigen.
[GB1443053A]
Claims (1)
1. CLAIMS: 1. A process for the isolation of a cancer associated polypeptide antigen (CAPA) comprising the steps: homogenizing CAPA-containing material in an aqueous solution at a temperature not above about 0 C separating solids from the mixture of liquid homogenate and solids resulting from step a) extracting said solids with an alkaline aqueous solution; ' . filtering the extract resulting from. step c) on a filtration gel of the molecular sieve type in bead form permitting fractionation of compounds havin 6 6 a molecular weight range including 10 · 10 to 20 · 10 , especially about 15 - 10^, eluting the gel and re- covering the 10 - 10 to 15* 10 fraction, especially the fraction of about 15 * 10 subjecting the fraction resulting from step d) to chromatography on a weak ion exchanger molecular sieve type gel to adsorb thereon impurities and recovering the first fraction leaving said exchanger; subjecting said first fraction to isoelectric precipitation; mixing the resulting precipitate with a molecular sieve type gel and subjecting said gel to pH-gradient elution; and, while decreasing the pH, recovering the fraction down to pH about 3 containing CAPA therein having a spectrophotometry absorption peak wave length at 229^233 nra and a molecular weight wlthiri the 2. A process according to claim 1, wherein the fraction resulting from the pH-gradient elution is subjected to gel filtration on a gel column, the eluted fractions of antigen having a spectrophotometric absorption peak wave length at 229-233 nm and a molecular weight within the range of about 20,000 - 27,000 being recovered. 3· A process according to claim 1, wherein the homogenate resulting from step a) is subjected to organic solvent treatment in the cold before step b). 4. A process according to claim 3, wherein the solvent used is ethyl ether. 5· A process according to claim 1, wherein the homogenization is carried out in water at a temperature not above about 0°C. 6. A process according to claim 1, wherein the solids resulting from step b) are lyophilized and then ground in a steel ball mill in the cold. 7· A process according to claim 6, wherein the grinding takes place at low temperature. 8. A process according to claim 6, wherein the grinding takes place at a temperature below the freezing point of the material under treatment. 9· A process according to claim 6, wherein the grinding takes place at a temperature of about -70°C. 10. A process according to claim 1, wherein under step d) the filtering is carried out on a gel selected from the group consisting of polyacrylamide gels, cross-linked dextran gels, agar and agarose gels, the gel being equili 42594/2 11. A process according to claim 1, wherein under step e) the chromatography is carried out on a column of a weak ion exchanger molecular sieve type gel at neutral pH. 12. A process according to claim 11, wherein the chromatography is carried out on a weak ion exchanger molecular sieve type polyacrylamide gel, said gel being in the form of a column at a neutral pH. 13. A process according to claim 1, wherein under step g) there is used a gel selected from the group consisting of polyacrylamide gels, cross-linked dextran gels, agar and agarose gels. 14. A process according to claim 2, wherein said gel filtration is carried out on a gel selected from the group consisting of polyacrylamide gel and cross-linked dextran gel. 15. A process according to claim 1, wherein the aqueous extract resulting from step c) is subjected to rapid heating to a temperature within the range of about 95 to about 100°C to destroy enzymes. 16. A process according to claim IS, whr-r> 18. Cancer associated polypeptide antigen (CAPA) having a molecular weight of 23,200 - 2,500 (S.D. ) and ehowing a spectrophotometric peak absorption at a wave length within the range from about 229 nm to about 233 nm, said polypeptide being based on a single peptide chain as shown by treatment with performic acid, and, if not protected by complexing with albumen, denaturating irreversibly at pH' s exceeding about 5. 19. CAPA according to claim l8, wherein the polypeptide comprises the following amino acids, the mole percentages thereof being as follows: Alanine 8.62 Arginine 4.57 Aspartic acid 10.39 Cysteine 0.95 Glutamic acid 17.0 Glycine 6.87 Histidine 1.00 Isoleucine 4.75 Leucine 10.49 Lysine 3-69 Methionine 1.91 Phenylalanine 2.75 Serine 7·74 Threonine 5.92 Tyrosine 3.21 Valine 6. 6 20. CAPA according to claim l8, comprising a fluorescent group emitting fluorescent light at about 350 nm when activated at a wavelength of about 288 nm. 21. A process for preparing antibodies monospecific with regard to CAPA, comprising the steps; a) preparing an aqueous solution at a pH less than about 3 of the CAPA as claimed in claim l8; b) preparing an oil emulsion, wherein the solution resulting from step a) is enclosed phase so as to be protected by the surrounding oil phase; c) injecting said oil emulsion into a living animal body, whereby the CAPA carried by the emulsion is transported to antibody-producing cells. 22. A process according to claim 21, wherein under step b) a Freund' s adjuvant is used for preparing the oil emulsion. 23. A process according to claim 21, wherein under step a) the aqueous solution is prepared at a pH lower than about 3 using as an acidifying agent a weak acid. 24. A process according to claim 3* wherein the weak acid used is formic acid. 25. A method of determining the presence of CAPA at different, stages of cancer progress by investigating material selected from the group consisting of serum, tissues, • ■ 42594/2 samples of said material by serial dilution; b) adding to each of said samples a predetermined amount of antiserum containing antibodies specific to the antigen; c) adding, after incubation', to each of said incubated samples a predetermined amount of stabilized (complexed) CAPA supported by a particulate carrier; d) comparing the resulting series of treated samples with control samples of decreasing known amounts of stabilized (complexed) CAPA providing inhibition and predetermined amounts of antiserum containing said antibodies and thereafter adding to each of said control samples a predetermined amount of CAPA supported by a particulate carrier; and e) establishing by comparison of said sample series and said control samples the amount of CAPA in the material of said living animal body to indicate the presence of cancer and its stage of progress. 26. A method according to claim 25, wherein said investigated material is patient serum,. 27· A process according to claim 1, wherein said antigen-containing material is tissue from human placenta. 28. A process according to claim 1, wherein said antigen-containing material is human tumor tissue. 29. A process according to claim 1, wherein said antigen-containing material is a culture of cancerous cells grown in vitro. JO. A method according to claim 25, wherein said investigated material is selected from the group consisting of biopsy material, surgical specimens, punctions and smears. 31. A method according to claim 25, wherein the polypeptide antigen used is that claimed in claim l8. 42594/2 32. A, method .-according to claim 25, wherein said investigated material under step a) is absorbed on a particulate carrier selected from the group consisting of: sheep blood red cells, latex, bentonite and collodion. 33· A method according to claim 25, wherein the blood cells used under step c) are sheep bloocT red" cells. y\. A method according to claim 25, wherein the antiserum used under step b) is derived from animals immunized with CAPA-containing material. . 35· A method according to claim 4, wherein the immunized animal is selected from the group consisting of horse and rabbit. 36. A composition useful as an immunizing agent, comprising as an active ingredient CAPA in combination with a pharmaceutically acceptable carrier. 37· A composition according to claim >6, comprising an oil emulsion, wherein an aqueous solution of a pH lower than about 3 containing CAPA constitutes the enclosed phase so as to be protected by the surrounding oil phase. 38. A composition according to claim 36, wherein the oil emulsion is based on Freund' s adjuvant. 39. A composition according to claim 36 comprising CAPA and a stabilizing amount of albumen in admixture therewith. 40. A composition according to claim 39, wherein the ratio of albumen to CAPA is at least 200:1 by weight. 41. A method of making a CAPA-albumen composition according to claim 39, comprising mixing in acid solution CAPA and albumen, and raising the pH of the solution to cause interaction between the components. 42594/2. „ A method according to claim 41 including the fur_th.er_.s.tep. of lyophilizing the composition. 43. diagnostic composition comprising a particulate material la¾elled_¾ th .albuma^-stahilized CAPA according to claim 39» 44. A diagnostic composition according to claim 43» wherein the particulate material is selected from the group consisting of tanned red "blood cells, latex, hentonite and collodion.
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US27027372A | 1972-07-10 | 1972-07-10 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IL42594A0 IL42594A0 (en) | 1973-08-29 |
| IL42594A true IL42594A (en) | 1976-08-31 |
Family
ID=23030635
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL42594A IL42594A (en) | 1972-07-10 | 1973-06-25 | Cancer associated polypeptide antigen,its preparation,its detection and immunizing compositions containing it |
Country Status (22)
| Country | Link |
|---|---|
| JP (2) | JPS5817168B2 (en) |
| AR (1) | AR197243A1 (en) |
| AT (1) | AT336780B (en) |
| BE (1) | BE802126A (en) |
| BR (1) | BR7305142D0 (en) |
| CA (1) | CA1039650A (en) |
| CH (1) | CH617853A5 (en) |
| DD (2) | DD118946A5 (en) |
| DE (2) | DE2333740C2 (en) |
| DK (1) | DK139898B (en) |
| ES (1) | ES416726A1 (en) |
| FI (1) | FI60567C (en) |
| FR (1) | FR2191885B1 (en) |
| GB (2) | GB1443053A (en) |
| IL (1) | IL42594A (en) |
| IN (1) | IN138903B (en) |
| IT (1) | IT1009527B (en) |
| NL (1) | NL7309257A (en) |
| NO (1) | NO146338C (en) |
| SE (3) | SE440697B (en) |
| SU (1) | SU581842A3 (en) |
| ZA (1) | ZA734632B (en) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4132769A (en) * | 1974-10-30 | 1979-01-02 | Osther Kurt B | Cancer antigen, cancer therapy, and cancer diagnosis |
| US4146603A (en) * | 1977-02-18 | 1979-03-27 | Research Corporation | Tumor specific glycoproteins and method for detecting tumorigenic cancers |
| US4172124A (en) * | 1978-04-28 | 1979-10-23 | The Wistar Institute | Method of producing tumor antibodies |
| JPS56145297A (en) * | 1980-04-11 | 1981-11-11 | Kureha Chem Ind Co Ltd | Preparative method of glycoprotein having immunosupressing activity |
| EP0087898A1 (en) * | 1982-02-22 | 1983-09-07 | Cancer Research Campaign Technology Limited | Antibodies and antigens useful in the diagnosis and treatment of cancer |
-
1973
- 1973-06-25 IL IL42594A patent/IL42594A/en unknown
- 1973-06-25 SE SE7308917A patent/SE440697B/en unknown
- 1973-06-25 IN IN1473/CAL/73A patent/IN138903B/en unknown
- 1973-06-29 FI FI2099/73A patent/FI60567C/en active
- 1973-07-03 DE DE2333740A patent/DE2333740C2/en not_active Expired
- 1973-07-03 DE DE2366609A patent/DE2366609C2/de not_active Expired
- 1973-07-03 NL NL7309257A patent/NL7309257A/xx not_active Application Discontinuation
- 1973-07-06 AR AR248979A patent/AR197243A1/en active
- 1973-07-06 CH CH988073A patent/CH617853A5/en not_active IP Right Cessation
- 1973-07-06 DD DD186676*A patent/DD118946A5/xx unknown
- 1973-07-06 DD DD172110A patent/DD113918A5/xx unknown
- 1973-07-09 GB GB3263473A patent/GB1443053A/en not_active Expired
- 1973-07-09 CA CA175,995A patent/CA1039650A/en not_active Expired
- 1973-07-09 NO NO2807/73A patent/NO146338C/en unknown
- 1973-07-09 IT IT26346/73A patent/IT1009527B/en active
- 1973-07-09 ES ES416726A patent/ES416726A1/en not_active Expired
- 1973-07-09 DK DK380773AA patent/DK139898B/en not_active IP Right Cessation
- 1973-07-09 GB GB4980974A patent/GB1443054A/en not_active Expired
- 1973-07-09 AT AT600773A patent/AT336780B/en not_active IP Right Cessation
- 1973-07-10 JP JP48077839A patent/JPS5817168B2/en not_active Expired
- 1973-07-10 SU SU7301949792A patent/SU581842A3/en active
- 1973-07-10 BE BE133300A patent/BE802126A/en not_active IP Right Cessation
- 1973-07-10 ZA ZA734632A patent/ZA734632B/en unknown
- 1973-07-10 FR FR7325241A patent/FR2191885B1/fr not_active Expired
- 1973-07-10 BR BR5142/73A patent/BR7305142D0/en unknown
-
1976
- 1976-09-06 SE SE7609836A patent/SE418186B/en not_active IP Right Cessation
- 1976-09-06 SE SE7609837A patent/SE440597B/en not_active IP Right Cessation
-
1981
- 1981-01-14 JP JP56003331A patent/JPS6018011B2/en not_active Expired
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