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Titolo:
DETERMINATION OF THE DISULFIDE BRIDGES IN FACTOR VA LIGHT-CHAIN
Autore:
XUE JC; KALAFATIS M; MANN KG;
Indirizzi:
UNIV VERMONT,DEPT BIOCHEM,HLTH SCI COMPLEX BURLINGTON VT 05405 UNIV VERMONT,DEPT BIOCHEM,HLTH SCI COMPLEX BURLINGTON VT 05405
Titolo Testata:
Biochemistry
fascicolo: 22, volume: 32, anno: 1993,
pagine: 5917 - 5923
SICI:
0006-2960(1993)32:22<5917:DOTDBI>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; ACTIVATED PROTEIN-C; FACTOR-XA; HUMAN CERULOPLASMIN; FACTOR-VIII; INTERNAL TRIPLICATION; COMPLETE CDNA; BINDING; EXPRESSION; DOMAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
J.C. Xue et al., "DETERMINATION OF THE DISULFIDE BRIDGES IN FACTOR VA LIGHT-CHAIN", Biochemistry, 32(22), 1993, pp. 5917-5923

Abstract

The 74-kDa light chain of bovine factor Va is composed of three domains: the NH2-terminal A3 domain and the COOH-terminal C1 and C2 domains. In total, the light chain has eight cysteines: two in the A3 domain and three in each C domain. To determine the locations of the disulfide bridges, peptides were obtained from factor Va and iodo [1-C-14] acetamide-labeled factor Va light chains by digestion with trypsin, activated protein C, lysylendopeptidase, and V8 protease. After HPLC purification, amino acid sequence and composition analyses showed that each domain of bovine Va light chain possesses a disulfide bond. The sites are Cys1684-Cys1710(A3), Cys1866-Cys2020 (C1), and Cys2025-Cys2180(C2). One free cysteine is located in each C domain, i.e., Cys1953 and Cys2100. The locations of the disulfide bonds in human Va and VIIIa lightchains are anticipated to be similar to those of bovine Va light chain, because the cysteines involved are conserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 10:15:44