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Enzymatic cleavage of cell surface proteins of pig and cow erythrocytes and its effect on concanavalin-mediated agglutinability

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Title Enzymatic cleavage of cell surface proteins of pig and cow erythrocytes and its effect on concanavalin-mediated agglutinability
 
Creator Sharma, Savita
Gokhale, Sadashiv M
 
Subject Agglutination
Mammalian erythrocyte
Membrane proteins
Glycophorins
Proteinases
Neuraminidase
 
Description 378-387
Study was carried out to understand and
compare architecture of the proteins of erythrocyte cell surface of some
mammals viz., Homo sapiens (human), Sus scorfa domestica (pig) and Bos taurus domestica
(cow). In this study, we investigated the action of proteinases viz.,
trypsin and chymotrypsin and neuraminidase on the erythrocyte surface proteins
and erythrocyte agglutination tendency with a lectin (concanavalin A). The
electrophoretic pattern of membrane proteins and glycophorins (analyzed by
SDS-PAGE and visualized by Coomassie brilliant blue and periodic acid-schiff
stains, respectively) and concanavalin A (Con A) agglutinability revealed that:
(i) There were variations in the number and molecular weights of glycophorins
in human, pig and cow, (ii) trypsin action on pig and cow erythrocyte membrane
proteins was similar, unlike human, (iii) glycophorins degradation by trypsin
and chymotrypsin was not similar in pig, as compared to that of human and cow,
(iv) erythrocytes agglutination with Con A was significantly different due to
differences in membrane composition and alterations in the surface proteins
after enzyme treatment, (v) a direct correlation was found between degradation
of glycophorins and Con A agglutinability, and (vi) removal of erythrocyte
surface sialic acids by neuraminidase specifically indicated an increase in Con
A agglutinability of pig and cow erythrocytes, similar to human.
 
Date 2014-11-12T11:03:00Z
2014-11-12T11:03:00Z
2014-10
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/29887
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.51(5) [October 2014]