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Title: Structural and functional characterization of a P-III metalloproteinase, leucurolysin-B, from Bothrops leucurus venom
Authors: Sanchez, Eladio F.
Gabriel, Lucilene M.
Gontijo, Silela
Gremski, Luiza H.
Veiga, Silvio S.
Evangelista, Karla S.
Eble, Johannes A.
Richardson, Michael
Ezequiel Dias Fdn
Univ Fed Parana
Univ Munster
Hosp Santa Casa
Universidade Federal de São Paulo (UNIFESP)
Keywords: leucurolysin-B
disintegrin-like protein
snake venom
Bothrops leucurus
Issue Date: 15-Dec-2007
Publisher: Elsevier B.V.
Citation: Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 468, n. 2, p. 193-204, 2007.
Abstract: Leucurolysin-B (leuc-B) is an hemorrhagic metalloproteinase found in the venom of Bothrops leucurus (white-tailed-jararaca) snake. By means of liquid chromatography consisting of gel filtration on Sephracryl S-200, S-300 and ion-exchange on DEAE Sepharose, leuc-B was purified to homogeneity. the proteinase has an apparent molecular mass of 55 kDa as revealed by the reduced SDS-PAGE, and represents approximately 1.2% of the total protein in B. leucurus venom. the partial amino acid sequence of leuc-B was determined by automated Edman sequencing of peptides derived from digests of the S-reduced and alkylated protein with trypsin. Leuc-B exhibits the characteristic motif of metalloproteinases, HEXXHXXGXXH and a methonine-containing turn of similar conformation (Metturn), which forms a hydrophobic basis for the zinc ions and the three histidine residues involved as ligands. Leuc-B has been characterized as a P-III metalloproteinase and possesses a multidomain structure including a metalloproteinase, a disintegrin-like (ECD sequence instead of the typical RGD motif) and a cysteine-rich C-terminal domain. Leuc-B contains three potential sites of N-glycosylation. the enzyme only cleaves the Ala(14)-Leu(15) peptide bond of the oxidized insulin B-chain and preferentially hydrolyzes the A alpha-chain of fibrinogen and the a-chain of fibrin. Its proteolytic activity was completely inhibited by metal chelating agents but not by other typical proteinase inhibitors. in addition, its enzymatic activity was stimulated by the divalent cations Ca2+ and Mg2+ but inhibited by Zn2+ and CU2+. the catalytic activity of leuc-B on extracellular matrix proteins could readily lead to loss of capillary integrity resulting in hemorrhage occurring at those sites (MHD = 30 ng in rabbit), with alterations in platelet function. in summary, here we report the isolation and the structure-function relationship of a P-III snake venom metalloproteinase. ((c)) 2007 Elsevier Inc. All rights reserved.
ISSN: 0003-9861
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