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Purification and characterization of serum α<sub>2</sub>-globulin binding protein from <i>Alocasia macrorhiza </i>tuber

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Title Purification and characterization of serum α2-globulin binding protein from Alocasia macrorhiza tuber
 
Creator Nayak, B Shivananda
Shivaraj, B
 
Description 227-234
A protein capable of precipitating serum
α2-globulin was purified from Alocasia macrorhiza tuber. The
protein, designated as Alocasia protein was heat labile and was found to exist
in four isomeric forms, each having four subunits. The serum α2-globulin
binding activity of the Alocasia protein was not altered by the action of
proteolytic enzymes like trypsin, chymotrypsin and pepsin .Unlike the naturally
occurring lectins, the Alocasia protein failed to agglutinate erythrocytes,
leukocytes and the microbial organisms. In addition, different

sugars and sugar derivatives did not
prevent the complex formation between the Alocasia protein and α2-globulin
of serum. Divalent metal ions and SH agents did not affect the activity of the
protein. Preliminary studies indicated that haptoglobin and α2-macroglobulins
were the major, if not the exclusive proteins that are responsible for
interaction with the purified Alocasia protein.
 
Date 2013-07-16T08:36:58Z
2013-07-16T08:36:58Z
2000-08
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/19826
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.37(4) [August 2000]