Characterization of malate dehydrogenase: Electrophoresis, isoelectric focusing, thermostability, inhibition and activity studies on homogenates of various organs of Biomphalaria glabrata (mollusca: pulmonata)

Author(s):  
Sudhir Narang ◽  
Neelam Narang
1990 ◽  
Vol 111 (4) ◽  
pp. 1639-1643 ◽  
Author(s):  
S C Ho ◽  
M Schindler ◽  
J L Wang

Extracts of Bradyrhizobium japonicum were fractionated on Sepharose columns covalently derivatized with lactose. Elution of the material that was specifically bound to the affinity column with lactose yielded a protein of Mr approximately 38,000. Isoelectric focusing of this sample yielded two spots with pI values of 6.4 and 6.8. This protein specifically bound to galactose-containing glycoconjugates, but did not bind either to glucose or mannose. Derivatives of galactose at the C-2 position showed much weaker binding; there was an 18-fold difference in the relative binding affinities of galactose versus N-acetyl-D-galactosamine. These results indicate that we have purified a newly identified carbohydrate-binding protein from Bradyrhizobium japonicum, that can exquisitely distinguish galactose from its derivatives at the C-2 position.


Biochemistry ◽  
1994 ◽  
Vol 33 (39) ◽  
pp. 11692-11698 ◽  
Author(s):  
C. Lindbladh ◽  
M. Rault ◽  
C. Hagglund ◽  
W. C. Small ◽  
K. Mosbach ◽  
...  

1979 ◽  
Vol 33 (3) ◽  
pp. 329-342 ◽  
Author(s):  
Elspeth B. Smith ◽  
Heather S. Dietz ◽  
Isobel B. Craig

1997 ◽  
Vol 31 (8) ◽  
pp. 2037-2049 ◽  
Author(s):  
Ph. Schmitt ◽  
A.W. Garrison ◽  
D. Freitag ◽  
A. Kettrup

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