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Titolo:
The antihemorrhagic factor, erinacin, from the European hedgehog (Erinaceus europaeus), a metalloprotease inhibitor of large molecular size possessing ficolin/opsonin P35 lectin domains
Autore:
Omori-Satoh, T; Yamakawa, Y; Mebs, D;
Indirizzi:
Univ Frankfurt, Zentrum Rechtsmed, D-6000 Frankfurt, Germany Univ Frankfurt Frankfurt Germany D-6000 tsmed, D-6000 Frankfurt, Germany Japan Sci & Technol Corp, Bangkok, Thailand Japan Sci & Technol Corp Bangkok Thailand chnol Corp, Bangkok, Thailand Queen Saovabha Mem Inst, Thai Red Cross Soc, Bangkok, Thailand Queen Saovabha Mem Inst Bangkok Thailand d Cross Soc, Bangkok, Thailand Natl Inst Infect Dis, Dept Biochem & Cell Biol, Tokyo, Japan Natl Inst Infect Dis Tokyo Japan Dept Biochem & Cell Biol, Tokyo, Japan
Titolo Testata:
TOXICON
fascicolo: 11, volume: 38, anno: 2000,
pagine: 1561 - 1580
SICI:
0041-0101(200011)38:11<1561:TAFEFT>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIDELPHIS-VIRGINIANA SERUM; AMINO-ACID-SEQUENCE; COLLAGEN-LIKE; HEMORRHAGIC METALLOPROTEINASES; TRIMERESURUS-FLAVOVIRIDIS; MACROGLOBULIN INHIBITORS; VENOM METALLOPROTEINASE; FIBRINOGEN-LIKE; BITIS ARIETANS; VIPEROUS SNAKE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Mebs, D Univ Frankfurt, Zentrum Rechtsmed, D-6000 Frankfurt, Germany Univ Frankfurt Frankfurt Germany D-6000 -6000 Frankfurt, Germany
Citazione:
T. Omori-Satoh et al., "The antihemorrhagic factor, erinacin, from the European hedgehog (Erinaceus europaeus), a metalloprotease inhibitor of large molecular size possessing ficolin/opsonin P35 lectin domains", TOXICON, 38(11), 2000, pp. 1561-1580

Abstract

From muscle extracts of the European hedgehog, Erinaceus europaeus, an antihemorrhagic factor, erinacin, was purified by ammonium sulfate precipitation followed by chromatography on DEAE-cellulose, hydroxylapatite and gel filtration columns. A purification of approx. 1400-fold was achieved with an overall yield of 21% in antihemorrhagic activity. The molecular weight of erinacin determined by gel filtration was approx. 1000 kDa. SDS-PAGE of erinacin under reducing conditions indicates that it consists of two types of subunits, alpha and beta, with molecular weights of 37 and 35 kDa, respectively, in a ratio of 1:2. In the presence of 6 M guanidine-HCl, erinacin dissociates into alpha-subunits and beta-subunit decamers. From these results the subunit assembling of erinacin has been formulated as alpha(10).2 beta(10). The molecular weight of the subunits and of the beta-subunit decamer was confirmed by MALDI-TOF mass spectrometry. Erinacin inhibits the hemorrhagic and proteolytic activity of the major hemorrhagic metalloprotease from the venom of Bothrops jararaca. Complete inhibition was achieved in an equimolar mixture of inhibitor and enzyme suggesting an equimolar complex. Erinacin is not inhibiting serine proteases such as trypsin and chymotrypsin, itwas characterized to be a metalloprotease inhibitor. In electronmicroscopy, flower bouquet-like structures characteristic for some animal lectins were observed. Amino acid sequence analysis indicated that both subunits are almost identical and are composed of common amino terminal, collagen- and fibrinogen-like domains homologous to proteins of the ficolin/opsonin P35 lectin family. (C) 2000 Elsevier Science Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 05:03:30