CA2100355A1 - Enzyme de conversion de l'endotheline - Google Patents

Enzyme de conversion de l'endotheline

Info

Publication number
CA2100355A1
CA2100355A1 CA 2100355 CA2100355A CA2100355A1 CA 2100355 A1 CA2100355 A1 CA 2100355A1 CA 2100355 CA2100355 CA 2100355 CA 2100355 A CA2100355 A CA 2100355A CA 2100355 A1 CA2100355 A1 CA 2100355A1
Authority
CA
Canada
Prior art keywords
protein
endothelin
ece
activity
enzyme
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.)
Abandoned
Application number
CA 2100355
Other languages
English (en)
Inventor
Lynne H. Parker Botehlo
Maria C. Garrigan
Anthony Johns
Barry L. Levinson
Kathleen C. Patterson
Mark A. Polokoff
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Berlex Laboratories Inc
Original Assignee
Individual
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Individual filed Critical Individual
Publication of CA2100355A1 publication Critical patent/CA2100355A1/fr
Abandoned legal-status Critical Current

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/48Hydrolases (3) acting on peptide bonds (3.4)
    • C12N9/50Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
    • C12N9/64Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
    • C12N9/6421Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
    • C12N9/6489Metalloendopeptidases (3.4.24)
    • C12N9/6497Endothelin-converting enzyme (3.4.24.71)
    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12YENZYMES
    • C12Y304/00Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
    • C12Y304/24Metalloendopeptidases (3.4.24)
    • C12Y304/24071Endothelin-converting enzyme 1 (3.4.24.71)

Landscapes

  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Organic Chemistry (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Genetics & Genomics (AREA)
  • Biochemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • General Engineering & Computer Science (AREA)
  • Biomedical Technology (AREA)
  • Medicinal Chemistry (AREA)
  • Molecular Biology (AREA)
  • Biotechnology (AREA)
  • Microbiology (AREA)
  • Enzymes And Modification Thereof (AREA)
CA 2100355 1991-02-04 1992-02-04 Enzyme de conversion de l'endotheline Abandoned CA2100355A1 (fr)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
US65039491A 1991-02-04 1991-02-04
US07/650,394 1991-02-04

Publications (1)

Publication Number Publication Date
CA2100355A1 true CA2100355A1 (fr) 1992-08-05

Family

ID=24608722

Family Applications (1)

Application Number Title Priority Date Filing Date
CA 2100355 Abandoned CA2100355A1 (fr) 1991-02-04 1992-02-04 Enzyme de conversion de l'endotheline

Country Status (3)

Country Link
EP (1) EP0575405A1 (fr)
CA (1) CA2100355A1 (fr)
WO (1) WO1992013944A1 (fr)

Families Citing this family (12)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0545344B1 (fr) * 1991-11-29 1997-05-02 Nisshin Flour Milling Co., Ltd. Enzymes de conversion d'endothéline
WO1994028012A1 (fr) * 1993-05-28 1994-12-08 Warner-Lambert Company Hydroxamates inhibiteurs de l'enzyme de conversion de l'endotheline
IT1266570B1 (it) * 1993-07-30 1997-01-09 Zambon Spa Derivati della propanammide n-eteroaril sostituiti utili nel trattamento delle malattie cardiovascolari
EP0638643A1 (fr) * 1993-08-13 1995-02-15 Nisshin Flour Milling Co., Ltd. Enzyme de conversion de l'endotheline et procédé pour la produire
KR950008684A (ko) * 1993-09-21 1995-04-19 쇼다 오사무 아포리포프로틴 b로 이루어진 엔도텔린 전환효소
AU8107094A (en) * 1993-11-16 1995-06-06 Basf Aktiengesellschaft Endothelin-converting enzyme
GB9325221D0 (en) * 1993-12-09 1994-02-09 Zeneca Ltd Nucleid acid
GB2284607A (en) * 1993-12-09 1995-06-14 Zeneca Ltd Mammalian endothelin converting enzyme and cDNA thereof
SE9403915D0 (sv) * 1994-11-14 1994-11-14 Annelie Almstedt Process A
US5658902A (en) * 1994-12-22 1997-08-19 Warner-Lambert Company Quinazolines as inhibitors of endothelin converting enzyme
DE60040089D1 (de) * 1999-11-19 2008-10-09 Solvay Pharm Bv Menschliches homolog aus der familie der metalloproteasen
JP2004524818A (ja) * 2000-10-04 2004-08-19 レキシコン・ジェネティクス・インコーポレーテッド 新規プロテアーゼおよびそれをコードするポリヌクレオチド

Also Published As

Publication number Publication date
EP0575405A1 (fr) 1993-12-29
EP0575405A4 (fr) 1994-03-02
WO1992013944A1 (fr) 1992-08-20

Similar Documents

Publication Publication Date Title
Ohnaka et al. Purification and characterization of a phosphoramidon-sensitive endothelin-converting enzyme in porcine aortic endothelium. OFF.
Beldent et al. Proteolytic release of human angiotensin-converting enzyme. Localization of the cleavage site.
Morty et al. Oligopeptidase B from Trypanosoma evansi: a parasite peptidase that inactivates atrial natriuretic factor in the bloodstream of infected hosts
Lanzillo et al. Angiotensin-converting enzyme from human tissues. Physicochemical, catalytic, and immunological properties.
US5712144A (en) Cloned factor C cDNA of the Singapore Horseshoe Crab, Carcinoscorpius rotundicauda and purification of Factor C proenzyme
Georgieva et al. Comparative analysis of the venom proteomes of Vipera ammodytes ammodytes and Vipera ammodytes meridionalis
Mignogna et al. BSTI, a trypsin inhibitor from skin secretions of Bombina bombina related to protease inhibitors of nematodes
Condra et al. Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii
CA2100355A1 (fr) Enzyme de conversion de l'endotheline
PL171907B1 (pl) Sposób wytwarzania dimeru Apolipoproteiny AL-Milano PL PL PL
Chapus et al. Stabilization of the C‐terminal part of pig and horse colipase by carboxypeptidase and trypsin inhibitors
Winkler et al. Purification and characterization of recombinant single-chain urokinase produced in Escherichia coli
Schatteman et al. Proteolytic activation of purified human procarboxypeptidase U
Cintra et al. Primary structure and biological activity of bradykinin potentiating peptides from Bothrops insularis snake venom
US5968764A (en) Glucose transporter vesicle aminopeptidase
Imada et al. Atrioactivase, a specific peptidase in bovine atria for the processing of pro-atrial natriuretic factor. Purification and characterization.
EP0263608A2 (fr) Protéine ayant des propriétés anticoagulantes et antimétastasiques
Silberring et al. A novel bovine spinal cord endoprotease with high specificity for dynorphin B
Retzios et al. Fibrinolytic enzymes from the venoms of Agkistrodon contortrix contortrix and Crotalus basiliscus basiliscus: cleavage site specificity towards the α-chain of fibrin
Halila et al. Purification of human procollagen type III N-proteinase from placenta and preparation of antiserum
US6025330A (en) Inhibitors of fibrin cross-linking and/or transglutaminases
Braun et al. Preparation and characterization of proteolyzed forms of human α-thrombin
Billadello et al. Characterization of MB creatine kinase isoform conversion in vitro and in vivo in dogs.
Larsson et al. The identity and properties of two forms of activated colipase from porcine pancreas
Angermann et al. Purification and characterization of human salivary‐gland prokallikrein from recombinant baculovirus‐infected insect cells

Legal Events

Date Code Title Description
FZDE Dead