Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
PRIMARY STRUCTURE OF A COAGULANT ENZYME, BILINEOBIN, FROM AGKISTRODONBILINEATUS VENOM
Autore:
NIKAI T; OHARA A; KOMORI Y; FOX JW; SUGIHARA H;
Indirizzi:
MEIJO UNIV,FAC PHARM,DEPT MICROBIOL,TEMPAKU KU,YAGOTOYAMA 150 NAGOYA AICHI 468 JAPAN MEIJO UNIV,FAC PHARM,DEPT MICROBIOL,TEMPAKU KU NAGOYA AICHI 468 JAPAN UNIV VIRGINIA,HLTH SCI CTR,BIOMOLEC RES FACIL CHARLOTTESVILLE VA 22908
Titolo Testata:
Archives of biochemistry and biophysics
fascicolo: 1, volume: 318, anno: 1995,
pagine: 89 - 96
SICI:
0003-9861(1995)318:1<89:PSOACE>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
PULSED AMPEROMETRIC DETECTION; THROMBIN-LIKE ENZYME; CHROMATOGRAPHY; PURIFICATION;
Keywords:
BILINEOBIN; COAGULANT ENZYME; SERINE PROTEASE; PRIMARY STRUCTURE; GLYCOPROTEIN; A-BILINEATUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
T. Nikai et al., "PRIMARY STRUCTURE OF A COAGULANT ENZYME, BILINEOBIN, FROM AGKISTRODONBILINEATUS VENOM", Archives of biochemistry and biophysics, 318(1), 1995, pp. 89-96

Abstract

The amino acid sequence and disulfide bridge location of the coagulant enzyme, named bilineobin, isolated from the venom of Agkistrodon bilineatus was determined by Edman sequencing of the peptides derived from digests with cyanogen bromide, clostripain, Staphylococcus aureus V8protease, trypsin, and chymotrypsin. This enzyme has a molecular weight of 57,000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; however, bilineobin consists of 235 amino acids and has a calculated molecular weight of 26,481, The enzyme contains fucose, GlcNAc,galactose, mannose and NeuAc and six N-linked glycosylation consensussites. The carboxyterminal amino acid, proline, was determined using carboxypeptidase Y. The six disulfide bonds of bilineobin link Cys(78)to Cys(234), Cys(120) to Cys(188), Cys(178) to Cys(203), Cys(7) to Cys(141), Cys(152) to Cys(167), and Cys(28) to Cys(44). The amino acid sequence similarity to flavoxobin (T. C. Shieh et al., 1988, J. Biochem(Tokyo) 103, 596-605) and batroxobin (N. Itoh ed al., 1987, J. Biol. Chem. 262, 3132-3135) was 67%, The deglycosylated enzyme more rapidly generated fibrinopeptide A than native bilineobin. (C) 1995 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 03:13:51