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Characterization of a 59 kDa gelatin-binding fragment of buffalo plasma fibronectin

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Title Characterization of a 59 kDa gelatin-binding fragment of buffalo plasma fibronectin
 
Creator Ahmed, Nizamuddin
Swamy, Naganath
 
Description 113-118
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.
 
Date 2013-07-15T07:14:12Z
2013-07-15T07:14:12Z
2002-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/19761
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.39(2) [April 2002]