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Purification and characterization of a cysteine-rich secretory protein from Philodryas patagoniensis snake venom by María E. Peichoto; Stephen P. Mackessy; Pamela Teibler; Flávio L. Tavares; Paula L. Burckhardt; María C. Breno; Ofelia Acosta; Marcelo L. Santoro is a Environmental Science article available to read on EtoBox.

What is Purification and characterization of a cysteine-rich secretory protein from Philodryas patagoniensis snake venom about?

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.

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

It is typically read by researchers, students, and practitioners in Environmental Science.

Author
María E. Peichoto; Stephen P. Mackessy; Pamela Teibler; Flávio L. Tavares; Paula L. Burckhardt; María C. Breno; Ofelia Acosta; Marcelo L. Santoro
Publisher
Elsevier Science; Elsevier ; Elsevier BV (ISSN 1532-0456)
Published
2009
Language
EN
Field
Environmental Science (Physical Sciences)

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