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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Purification and characterization of a cysteine-rich secretory protein from Philodryas patagoniensis snake venom

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Author(s):
Peichoto, Maria E. [1, 2] ; Mackessy, Stephen P. [3] ; Teibler, Pamela [2] ; Tavares, Flavio L. [1] ; Burckhardt, Paula L. [4] ; Breno, Maria C. [4] ; Acosta, Ofelia [2] ; Santoro, Marcelo L. [1]
Total Authors: 8
Affiliation:
[1] Inst Butantan, Lab Fisiopatol, BR-05503900 Sao Paulo - Brazil
[2] Univ Nacl Nordeste, Catedra Farmacol, Fac Ciencias Vet, RA-3400 Corrientes - Argentina
[3] Univ No Colorado, Sch Biol Sci, Greeley, CO 80639 - USA
[4] Inst Butantan, Farmacol Lab, BR-05503900 Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY C-TOXICOLOGY & PHARMACOLOGY; v. 150, n. 1, p. 79-84, JUL 2009.
Web of Science Citations: 29
Abstract

Cysteine-rich secretory proteins (CRiSPs) are widespread in reptile venoms, but most have functions that remain unknown. In the present study we describe the purification and characterization of a CRiSP (patagonin) from the venom of the rear-fanged snake Philodryas patagoniensis, and demonstrate its biological activity. Patagonin is a single-chain protein, exhibiting a molecular mass of 24,858.6 Da, whose NH(2)-terminal and MS/MS-derived sequences are nearly identical to other snake venom CRiSPs. The purified protein hydrolyzed neither azocasein nor fibrinogen, and it could induce no edema, hemorrhage or inhibition of platelet adhesion and aggregation. In addition, patagonin did not inhibit contractions of rat aortic smooth muscle induced by high K(+). However, it caused muscular damage to murine gastrocnemius muscle, an action that has not been previously described for any snake venom CRiSPs. Thus, patagonin will be important for studies of the structure-function and evolutionary relationships of this family of proteins that are widely distributed among snake venoms. (C) 2009 Elsevier Inc. All rights reserved. (AU)

FAPESP's process: 08/02996-8 - Venoms from neonate and mature Bothrops jararaca snakes: comparison between enzymatic and biological activities, immunoneutralization, chemical composition and ability to induce hemostatic disorders
Grantee:Marcelo Larami Santoro
Support Opportunities: Regular Research Grants