Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/19761
Title: Characterization of a 59 kDa gelatin-binding fragment of buffalo plasma fibronectin
Authors: Ahmed, Nizamuddin
Swamy, Naganath
Issue Date: Apr-2002
Publisher: NISCAIR-CSIR, India
Abstract: Limited proteolysis of buffalo plasma fibronectin (FN) by thermolysin yielded four gelatin-binding fragments of which, the major 59 kDa fragment, GBFl, was isolated by gelatin-Sepharose and heparin-Sepharose affinity columns. GBFl appeared during early phase of thermolysin digestion and remained intact even after 4 hr of digestion. GBF1 may be similar to 56 kDa gelatin-binding fragment of FNs from human and hamster plasma. But, it is more resistant to thermolysin cleavage. The fragment binds to heparin with low affinity. On the basis of the structure of human plasma FN, the modular structure of GBFl may be given as: 6Fn1 1Fn2 2Fn2 7Fn1 8Fn1 9Fnl 1Fn3. Biophysical properties of GBF1 suggest an expanded native conformation. The interaction of the fragment with gelatin is pH-dependent and independent of NaCl concentration.
Page(s): 113-118
URI: http://hdl.handle.net/123456789/19761
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections: IJBB Vol.39(2) [April 2002]

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