Document Detail


Structural and functional properties of Cr 5, a new Lys49 phospholipase A2 homologue isolated from the venom of the snake Calloselasma rhodostoma.
MedLine Citation:
PMID:  17123155     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Cr 5 PLA(2) homologous (K49) was isolated from Calloselasma rhodostoma venom in only one chromatographic step in reverse phase HPLC (RP-HPLC) (on mu-Bondapack C-18). A molecular mass of 13.965 Da was determined by MALDI-TOF mass spectrometry. The amino acid composition showed that Cr 5 had a high content of Lys, Tyr, Gly, Pro, and 14 half-Cys residues, typical residues of a basic PLA(2). The complete amino acid sequence of Cr 5 PLA(2) contains 120 residues, resulting in a calculated pI value of 5.55. This sequence shows high identity values when compared to other K49 PLA(2)s isolated from the venoms of viperid snakes. Lower identity is observed in comparison to D49 PLA(2)s. The sequence found was SLVELGKMIL QETGKNPAKS YGAYGCNCGV LGRHKPKDAT DRCCFVHKCC YKKLTGCDPK KDRYSYSWKD KTIVCGENNP CLKEMCECDK AVAICLRENL DTYNKKYRYL KPFCKKADDC. In mice, Cr 5 induced myonecrosis and edema upon intramuscular and intravenous injections, respectively. The LD(50) of Cr 5 was 0.070 mg/kg of the animal weight, by intracerebroventricular (i.c.v.) route. In vitro, the toxin caused rapid cytolytic effect upon mouse skeletal muscle myoblasts in culture. The isolation of this PLA(2) and the combined structural and functional information obtained classify Cr 5 as a new member of the K49 PLA(2) family, since it presents typical features from such proteins.
Authors:
V L Bonfim; L A Ponce-Soto; J C Novello; S Marangoni
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The protein journal     Volume:  25     ISSN:  1572-3887     ISO Abbreviation:  Protein J.     Publication Date:  2006 Dec 
Date Detail:
Created Date:  2006-12-07     Completed Date:  2007-04-23     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  101212092     Medline TA:  Protein J     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  492-502     Citation Subset:  IM    
Affiliation:
Department of Biochemistry, Institute of Biology, State University of Campinas, P.O. Box 6109, 13083-970, Campinas, SP, Brazil.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Cells, Cultured
Crotalid Venoms / chemistry*
Edema / chemically induced
Mice
Molecular Sequence Data
Muscle Fibers, Skeletal / cytology,  drug effects
Myoblasts / cytology,  drug effects
Phospholipases A / chemistry,  isolation & purification*,  toxicity
Phospholipases A2
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Viperidae / metabolism*
Chemical
Reg. No./Substance:
0/Crotalid Venoms; EC 3.1.1.-/Phospholipases A; EC 3.1.1.4/Phospholipases A2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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