Change of enzyme properties caused by cross-linking treatment of human erythrocytes.

Abstract:

:Aragon et al [4] reported that rat erythrocytes can be cross-linked and permeabilized without significant inactivation or alterations of several enzymes in the glycolytic pathway. If this is the case, in situ kinetic analysis of the red cell enzymes in normal human red cells and abnormal red cells associated with hemolytic problems could be performed. However, we found that the treatment of human red cells with several bifunctional cross-linking reagents under various conditions always caused a certain extent of inactivation and a change in kinetic properties of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, and lactate dehydrogenase. Thus, the cross-linking and permeabilization method, as it stands, is not satisfactory for in situ kinetic analysis of red cell enzymes.

journal_name

Am J Hematol

authors

Ikawa M,Yoshida A

doi

10.1002/ajh.2830130103

subject

Has Abstract

pub_date

1982-08-01 00:00:00

pages

9-13

issue

1

eissn

0361-8609

issn

1096-8652

journal_volume

13

pub_type

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