Purification and characterization of a 34-kDa, heat stable glycoprotein from Synadenium grantii latex: action on human fibrinogen and fibrin clot

Rajesh, R. and Nataraju, A. and Raghavendra Gowda, C. D. and Frey, B. M. and Frey, F. J. and Vishwanath, B. S. (2006) Purification and characterization of a 34-kDa, heat stable glycoprotein from Synadenium grantii latex: action on human fibrinogen and fibrin clot. BIOCHIMIE, 88 (10). pp. 1313-1322.

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Official URL: http://dx.doi.org/10.1016/j.biochi.2006.06.007

Abstract

Latex glycoprotein (LGP) from Synadenium grantii latex was purified by the combination of heat precipitation and gel permeation chromatography. LGP is a heat stable protein even at 80 degrees C showed a sharp single band both in SDS-PAGE as well as in native (acidic) PAGE. LGP is a monomeric protein appears as single band under reducing condition. It is a less hydrophobic protein showed sharp single peak in R-P-HPLC with retention time of 13.3 m. The relative molecular mass of LGP is 34.4 kDa. CD spectrum of LGP explains less content of a-helix (7%), and high content of P-pleated sheets (48%) and random coils (46%). The N-tenninal sequence of LGP is D-F-P-S-D-W-Y-A-Y-E-G-Y-V-I-D-R-P-F-S. Purified LGP is a fibrinogen degrading protease hydrolyses all the three subunits in the order of A alpha, B beta and gamma. The hydrolytic pattern is totally different from plasmin as well as thrombin. LGP reduces recalcification time from 165 to 30 s with citrated human plasma but did not show thrombin like as well as factor Xa-like activity. Although LGP induces procoagulant activity, it hydrolyses partially cross-linked fibrin clot. It hydrolyses all the subunits of partially cross-linked fibrin clot (alpha- chains, beta-chain and gamma-gamma dimer). LGP is a serine protease, inhibited by PMSF. Other serine protease inhibitors, aprotinin and leupeptin did not inhibit the caseinolytic activity as well as fibrinogenolytic activity. We report purification and characterization of a glycoprotein from Synadenium grantii latex with human fibrino(geno)lytic activity. (c) 2006 Elsevier Masson SAS. All rights reserved.

Item Type: Article
Uncontrolled Keywords: Synadenium grantii; latex glycoprotein (LGP); hemostasis; fibrinogenolytic activity; fibrin clot hydrolyzing activity
Subjects: Agriculture Biological Sciences > Biochemistry
University of Mysore > PG Campuses > Manasagangotri, Mysore > Agriculture Biological Sciences > Biochemistry
Divisions: PG Campuses > Manasagangotri, Mysore > Biochemistry
Depositing User: Users 17 not found.
Date Deposited: 26 Apr 2013 13:50
Last Modified: 07 Aug 2013 07:48
URI: http://eprints.uni-mysore.ac.in/id/eprint/5068

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