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Titolo:
Isolation of a proteinase with plasminogen-activating activity from Lachesis muta muta (bushmaster) snake venom
Autore:
Sanchez, EF; Santos, CI; Magalhaes, A; Diniz, CR; Figueiredo, S; Gilroy, J; Richardson, M;
Indirizzi:
Fdn Ezequiel Dias, Ctr Pesquisa & Desenvolvimento, BR-30510010 Belo Horizonte, MG, Brazil Fdn Ezequiel Dias Belo Horizonte MG Brazil BR-30510010 BConte, MG, Brazil Univ Fed Espirito Santo, Dept Bioquim, Vitoria, ES, Brazil Univ Fed Espirito Santo Vitoria ES Brazil t Bioquim, Vitoria, ES, Brazil Univ Durham, Dept Biol Sci, Sci Labs, Durham DH1 3LE, England Univ DurhamDurham England DH1 3LE ci, Sci Labs, Durham DH1 3LE, England
Titolo Testata:
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
fascicolo: 1, volume: 378, anno: 2000,
pagine: 131 - 141
SICI:
0003-9861(20000601)378:1<131:IOAPWP>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
THROMBIN-LIKE ENZYME; AMINO-ACID-SEQUENCE; PURIFICATION; PA; FIBRINOGEN; THERAPY;
Keywords:
plasminogen activator; fibrinolysis; snake venom; Lachesis muta;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Sanchez, EF Fdn Ezequiel Dias, Ctr Pesquisa & Desenvolvimento, BR-30510010Belo Horizonte, MG, Brazil Fdn Ezequiel Dias Belo Horizonte MG Brazil BR-30510010 BCazil
Citazione:
E.F. Sanchez et al., "Isolation of a proteinase with plasminogen-activating activity from Lachesis muta muta (bushmaster) snake venom", ARCH BIOCH, 378(1), 2000, pp. 131-141

Abstract

A plasminogen activator enzyme (LV-PA) from Lachesis muta muta venom was purified to homogeneity using gel filtration and anion exchange chromatography, SDS-PAGE under reducing conditions showed a single protein band with anM-r of 33,000 Da, It is an acidic glycoprotein which activates plasminogento plasmin indirectly, functioning via prior formation of a molecular complex, known as plasminogen activator. The purified preparation catalyzes thehydrolysis of several p-nitroanilide peptide substrates containing Lys at the scissile bond. In contrast, no hydrolysis was detected on the syntheticsubstrates TAME and BAPNA, which contain arginine. By the use of the plasmin-specific chromogenic substrate Tos-Gly-Pro-Lys-pNA, the preparation had a plasmin-like activity of 0.68 U/mg, which was 35.8-fold higher than that of the crude venom from which it was prepared. In vitro, fibrin hydrolysis using LV-PA as plasminogen activator displayed more similarity with the effect produced by streptokinase (SK), SDS-PAGE (10%) analysis showed a 115-kDa complex formation after incubation of plasminogen with either LV-PA or SK, At a molar ratio of 50:1 (fibrinogen:enzyme), the preparation exhibited weakly fibrinogenolytic activity. However, LV-PA is distinguished from thrombin in that it does not clot fibrinogen. After incubation of LV-PA with platelet-rich plasma, the enzyme (2 mu M) showed no effect on platelet aggregation induced by ADP, epinephrine, or collagen. Comparison of the N-terminalsequence of LV-PA with other snake venom plasminogen activators revealed that LV-PA exhibits a high degree of sequence identity with the TsVPA from Trimeresurus stejnegeri (90%) and with the Haly-PA from Agkistrodon halys (85%). LV-PA also has homology with other snake venom serine proteinases suchas the thrombin-like/gyroxin analogue (38%) from bushmaster venom and withother coagulation serine proteases. The proteinase was readily inhibited by treatment with p-nitrophenyl p-guanidinebenzoate, p-aminobenzamidine, andphenylmethanesulfonyl fluoride but was not affected by metal chelators, (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/03/20 alle ore 19:13:44