SE8203674L - Sett att framstella en toxoid - Google Patents
Sett att framstella en toxoidInfo
- Publication number
- SE8203674L SE8203674L SE8203674A SE8203674A SE8203674L SE 8203674 L SE8203674 L SE 8203674L SE 8203674 A SE8203674 A SE 8203674A SE 8203674 A SE8203674 A SE 8203674A SE 8203674 L SE8203674 L SE 8203674L
- Authority
- SE
- Sweden
- Prior art keywords
- acid
- toxoid
- pseudomonas aeruginosa
- elastase
- activity
- Prior art date
Links
- 241000589517 Pseudomonas aeruginosa Species 0.000 claims abstract 4
- 102000016387 Pancreatic elastase Human genes 0.000 claims abstract 3
- 108010067372 Pancreatic elastase Proteins 0.000 claims abstract 3
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 claims 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 claims 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims 2
- 239000002253 acid Substances 0.000 claims 2
- 235000001014 amino acid Nutrition 0.000 claims 2
- 150000001413 amino acids Chemical class 0.000 claims 2
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 claims 1
- 239000004475 Arginine Substances 0.000 claims 1
- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-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
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-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
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-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
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 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
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims 1
- 238000000862 absorption spectrum Methods 0.000 claims 1
- 235000004279 alanine Nutrition 0.000 claims 1
- 229910021529 ammonia Inorganic materials 0.000 claims 1
- 239000000427 antigen Substances 0.000 claims 1
- 102000036639 antigens Human genes 0.000 claims 1
- 108091007433 antigens Proteins 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
- 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
- 239000007853 buffer solution Substances 0.000 claims 1
- 229960003067 cystine Drugs 0.000 claims 1
- 238000001962 electrophoresis Methods 0.000 claims 1
- 238000002523 gelfiltration 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
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims 1
- 239000000843 powder Substances 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 claims 1
- 102000004169 proteins and genes Human genes 0.000 claims 1
- 108090000623 proteins and genes Proteins 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
- 108091005804 Peptidases Proteins 0.000 abstract 1
- 239000004365 Protease Substances 0.000 abstract 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 abstract 1
- 208000015181 infectious disease Diseases 0.000 abstract 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6448—Elastases, e.g. pancreatic elastase (3.4.21.36); leukocyte elastase (3.4.31.37)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/12—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria
- C07K16/1203—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria
- C07K16/1214—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from bacteria from Gram-negative bacteria from Pseudomonadaceae (F)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/40—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against enzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Immunology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Claims (4)
1. -6-procentig formalin eller 0,25-5 M oximetansulfinsyra till att ge en toxoid mcd f6ljande fysikalisk-kemiska egenskaper: (I: molvikt: 47 000 (gelfiltrering)
2. ultraviolett absorptionsspektrum: maximum nn (g278 21,2, % 0,1 M KCl), minimum 252 mm1
3. isoelektrisk punkt: pH 6,5 (elektrofores med acetatfilM)
4. ingaende aminosyror: (aminosyra i 2/100 g protein) asparginsyra (14,2), tyrosin (9,9), fenylalanin (7,0), glotaminsyra (6,5), arginin (6,5), alanin (5,3), glycin (,6), serin (5,6), treonin (5,0), valin (4,9), leucin (4,3), lysin (3,9), meticnin (2,9), prolinisoleucin (2,7), histidin (2,6), trYptofan (g,S), cystin/2 (1,2), ammoniak (0,9) (totalt 94,7 g) (S) utseende: fArglost pulver 6. antigenaktivitet Orly 7. elastasaktivitet:ativ.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP1083676A JPS5296727A (en) | 1976-02-05 | 1976-02-05 | Toxoid of pseudomonas aeruginosa protease |
JP1083776A JPS5296728A (en) | 1976-02-05 | 1976-02-05 | Toxoid of pseudomonas aeruginosa elastase |
Publications (2)
Publication Number | Publication Date |
---|---|
SE8203674L true SE8203674L (sv) | 1982-06-14 |
SE442086B SE442086B (sv) | 1985-12-02 |
Family
ID=26346182
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
SE7701037A SE442269B (sv) | 1976-02-05 | 1977-02-01 | Sett att framstella en toxoid, avledd fran proteas fran pseudomona aeruginosa |
SE8203674A SE442086B (sv) | 1976-02-05 | 1982-06-14 | Sett att framstella en toxoid, avledd fran elastas fran pseudomonas aeruginosa |
Family Applications Before (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
SE7701037A SE442269B (sv) | 1976-02-05 | 1977-02-01 | Sett att framstella en toxoid, avledd fran proteas fran pseudomona aeruginosa |
Country Status (6)
Country | Link |
---|---|
US (1) | US4160023A (sv) |
CA (1) | CA1085293A (sv) |
CH (1) | CH628679A5 (sv) |
DE (1) | DE2704767A1 (sv) |
FR (1) | FR2362154A1 (sv) |
SE (2) | SE442269B (sv) |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CA1256370A (en) * | 1984-02-24 | 1989-06-27 | Yuzuru Homma | Toxoids of elastase of pseudomonas aeruginosa origin |
US5233024A (en) * | 1991-04-09 | 1993-08-03 | The Brigham & Women's Hospital | Anti-idiotypic monoclonal antibodies for mucoid pseudomonas aeruginosa, their preparation and use |
Family Cites Families (12)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US2528972A (en) * | 1947-05-15 | 1950-11-07 | Western Reserve University | Prophylactic toxoid compound and method of making same |
US3135662A (en) * | 1961-01-05 | 1964-06-02 | Burroughs Wellcome Co | Diphtheria toxoid preparation and its production |
US3658986A (en) * | 1969-07-02 | 1972-04-25 | Victor N Tompkins | Immunization methods against toxic effects of bacterial infection |
US3674863A (en) * | 1969-12-08 | 1972-07-04 | Parke Davis & Co | Polyvalent immunizing agents and methods for their production |
US3987164A (en) * | 1970-10-20 | 1976-10-19 | Yuzuru Homma | Method for prevention of pseudomonas aeruginosa infections |
US3928565A (en) * | 1971-10-19 | 1975-12-23 | Yuzuru Homma | Pharmaceutical preparation of pseudomonas aeruginosa bacterial component possessing anti-tumor and anti-infection properties |
FR2111719B1 (sv) * | 1970-10-20 | 1975-02-07 | Yuzuru Homma | |
FR2180594A1 (en) * | 1972-04-21 | 1973-11-30 | Research Corp | Reducing elastase - elaborating bacterial infection - using bacterial elastase as antigen |
FR2227861B1 (sv) * | 1973-05-04 | 1976-07-02 | Anvar | |
DE2340911A1 (de) * | 1973-08-13 | 1975-05-07 | Behringwerke Ag | Tetanus-antigen und verfahren zu seiner herstellung |
JPS51133489A (en) * | 1975-05-14 | 1976-11-19 | Tokyo Daigaku | Process for producing microbial components of pseudomonas aeruginosa h aving antimicrobial and antitumor activities |
JPS5296729A (en) * | 1976-02-05 | 1977-08-13 | Shionogi & Co Ltd | Mixed vaccin for cyanomycosis |
-
1977
- 1977-01-20 CA CA270,134A patent/CA1085293A/en not_active Expired
- 1977-01-31 US US05/764,454 patent/US4160023A/en not_active Expired - Lifetime
- 1977-02-01 SE SE7701037A patent/SE442269B/sv not_active IP Right Cessation
- 1977-02-04 CH CH140177A patent/CH628679A5/de not_active IP Right Cessation
- 1977-02-04 DE DE19772704767 patent/DE2704767A1/de active Granted
- 1977-02-04 FR FR7703275A patent/FR2362154A1/fr active Granted
-
1982
- 1982-06-14 SE SE8203674A patent/SE442086B/sv not_active IP Right Cessation
Also Published As
Publication number | Publication date |
---|---|
CH628679A5 (de) | 1982-03-15 |
SE442269B (sv) | 1985-12-16 |
FR2362154A1 (fr) | 1978-03-17 |
DE2704767C2 (sv) | 1987-07-23 |
DE2704767A1 (de) | 1977-08-18 |
FR2362154B1 (sv) | 1983-04-29 |
SE7701037L (sv) | 1977-08-06 |
CA1085293A (en) | 1980-09-09 |
SE442086B (sv) | 1985-12-02 |
US4160023A (en) | 1979-07-03 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Lord et al. | Laser-excited Raman spectroscopy of biomolecules: II. Native ribonuclease and α-chymotrypsin | |
Ohta et al. | Thermostable protease from thermophilic bacteria: I. thermostability, physicochemical properties, and amino acid composition | |
McLaren | Photochemistry of enzymes, proteins, and viruses | |
Phillips | The N-terminal groups of calf-thymus histones | |
Geisler et al. | Purification of smooth‐muscle desmin and a protein‐chemical comparison of desmins from chicken gizzard and hog stomach | |
Fujimaki et al. | Diffusable bitter peptides in peptic hydrolyzate of soybean protein | |
Maeda et al. | Some chemical properties of the venom of the rattlesnake, Crotalus viridis helleri | |
Smith et al. | Purification and properties of a c-type cytochrome from Micrococcus denitrificans | |
KR840006198A (ko) | 항원성 합성 펩타이드의 제조방법 | |
DE69723812D1 (de) | Aminosäurezusammensetzungen | |
Fry et al. | Isolation and partial characterization of a chromophore-peptide fragment from pepsin digests of phytochrome | |
Garfinkel et al. | Raman spectra of amino acids and related compounds. x. the raman spectra of certain peptides and of lysozyme1-3 | |
Burton et al. | Thymic hormone-like restoration by human prealbumin of azathioprine sensitivity of spleen cells from thymectomized mice. | |
Ruey et al. | Amino acid composition and specificity of a keratinase of Trichophyton mentagrophytes | |
SE8203674L (sv) | Sett att framstella en toxoid | |
SE8203912D0 (sv) | Forfarande for totalt eller partiellt avlegsnande av asparaginsyra och glutaminsyra fran proteinhydrolysat och blandningar av aminosyror samt aminosyrakompositioner erhallna genom forfarandet med hogt neringsverde | |
Dinamarca et al. | DDT-dehydrochlorinase II: Subunits, sulfhydryl groups, and chemical composition | |
Vivanco-Martinez et al. | Chemical modification of carboxyl groups in human Fcγ fragment: structural role and effect on the complement fixation | |
Marik et al. | Studies on phytohemagglutinins XVI. Subunit structure of the pea isophytohemagglutinins | |
NO942930D0 (no) | Forbindelser og produkter basert på Amadori-reaksjoner samt fremgangsmåte til fremstilling av bruk av samme | |
Hayakawa et al. | Copolymerization of the Leuchs anhydrides of the eighteen amino acids common to protein | |
Otey et al. | Studies on polycysteine peptides and proteins. II. Apparent dissociation constants, and ultraviolet and infrared absorption spectra of isomeric cystinylcystine peptides | |
HIRADO et al. | Purification and characterization of a bovine colostrum low molecular weight cysteine proteinase inhibitor | |
Abe et al. | Electrophoretical analysis of zein and isolation of its components | |
Jönsson | Purification and some properties of a protease from Alternaria tenuissima |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
NUG | Patent has lapsed |
Ref document number: 8203674-0 Effective date: 19910117 Format of ref document f/p: F |