Purification and characterization of a 34-kDa, heat stable glycoprotein from Synadenium grantii latex: action on human fibrinogen and fibrin clot
R Rajesh, A Nataraju, CDR Gowda, BM Frey, FJ Frey… - Biochimie, 2006 - Elsevier
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° 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 RP-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 …
heat precipitation and gel permeation chromatography. LGP is a heat stable protein even at
80° 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 RP-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 …
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