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Titolo:
MALDI-TOF mass spectrometry analysis of substrate specificity of lebetase,a direct-acting fibrinolytic metalloproteinase from Vipera lebetina snake venom
Autore:
Trummal, K; Vija, H; Subbi, J; Siigur, J;
Indirizzi:
Natl Inst Chem Phys & Biophys, EE-12618 Tallinn, Estonia Natl Inst Chem Phys & Biophys Tallinn Estonia EE-12618 Tallinn, Estonia
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
fascicolo: 2, volume: 1476, anno: 2000,
pagine: 331 - 336
SICI:
0167-4838(20000209)1476:2<331:MMSAOS>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
CROTALUS-BASILISCUS-BASILISCUS; HEMORRHAGIC METALLOPROTEINASES; SUBSTANCE-P; ENZYMES; METALLOENDOPEPTIDASES; PURIFICATION; STROMELYSIN;
Keywords:
lebetase; snake venom; fibrinolytic enzyme; MALDI-TOF mass spectrometry; substance P; substrate specificity;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
22
Recensione:
Indirizzi per estratti:
Indirizzo: Siigur, J Natl Inst Chem Phys & Biophys, Akad Tee 23, EE-12618 Tallinn, Estonia Natl Inst Chem Phys & Biophys Akad Tee 23 Tallinn Estonia EE-12618
Citazione:
K. Trummal et al., "MALDI-TOF mass spectrometry analysis of substrate specificity of lebetase,a direct-acting fibrinolytic metalloproteinase from Vipera lebetina snake venom", BBA-PROT ST, 1476(2), 2000, pp. 331-336

Abstract

Lebetase is a direct-acting fibrinolytic zinc metalloendopeptidase relatedin amino acid sequence to reprolysins which include both hemorrhagic and non-hemorrhagic proteinases. Despite apparent structural similarities, fibrinolytic and hemorrhagic proteinases differ significantly in substrate specificity. In this study, we have examined the activity of lebetase I against biologically active peptides (bradykinin, kallidin, substance P) and 6-10 amino acid residues containing peptides synthesized according to cleavage regions of alpha(2)-macroglobulin, pregnancy zone protein (PZP) and fibrinogen. Lebetase was found to have no activity against studied hexapeptides. Surprisingly, the best substrates for lebetase were substance P, and peptide fragment of PZP, both were cleaved at position Pro-Gin. Identification of the hydrolysis products of 15 peptides by MALDI-TOF mass spectrometry analysis indicates that lebetase possesses broad substrate specificity. The MALDI-TOF MS technique was proven to be highly efficient for the recovery and identification of the peptides released by lebetase hydrolysis. (C) 2000 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 11:45:47