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Titolo:
Molecular cloning and functional characterization of a snake venom metalloprotease
Autore:
Jeon, OH; Kim, DS;
Indirizzi:
Yonsei Univ, Coll Sci, Dept Biochem, Seoul 120749, South Korea Yonsei Univ Seoul South Korea 120749 Biochem, Seoul 120749, South Korea Yonsei Univ, Bioprod Res Ctr, Seoul 120749, South Korea Yonsei Univ Seoul South Korea 120749 Res Ctr, Seoul 120749, South Korea
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 2, volume: 263, anno: 1999,
pagine: 526 - 533
SICI:
0014-2956(199907)263:2<526:MCAFCO>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLATELET-AGGREGATION INHIBITOR; AMINO-ACID-SEQUENCE; CROTALUS-ATROX; HEMORRHAGIC METALLOPROTEINASES; EXTRACELLULAR-MATRIX; BOTHROPS-JARARACA; GENE FAMILY; DISINTEGRIN; CDNA; PURIFICATION;
Keywords:
disintegrin; enzyme processing; metalloprotease; protein refolding;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Kim, DS Yonsei Univ, Coll Sci, Dept Biochem, Seoul 120749, South Korea Yonsei Univ Seoul South Korea 120749 , Seoul 120749, South Korea
Citazione:
O.H. Jeon e D.S. Kim, "Molecular cloning and functional characterization of a snake venom metalloprotease", EUR J BIOCH, 263(2), 1999, pp. 526-533

Abstract

A cDNA clone, MT-d, encoding metalloprotease precursor was isolated from snake (Agkistrodon halys brevicaudus) venom gland cDNA library. MT-d-I protein containing both metalloprotease and disintegrin domains, and MT-d-II protein containing the metalloprotease domain only were expressed in Escherichia coli and refolded successfully into their functional forms. Each of the refolded enzyme species exhibited distinct substrate specificity. Proteolytic activity of the MT-d-1 was able to hydrolyse type I gelatin, type-III and V collagens in contrast with the catalytic function of MT-d-II. MT-d-I protein having metalloprotease activity was also able to inhibit platelet aggregation. Functionally active MT-d-I protein underwent autoproteolytic processing in vitro to produce metalloprotease and disintegrin; this processingwas accompanied by significant changes in the substrate specificity of theenzyme activity. Experimental evidence strongly suggests that the disintegrin domain in the metalloprotease precursor modulates the. catalytic function of the enzyme in hydrolysing extracellular matrix proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 16/07/20 alle ore 05:57:11