Accession Number:

ADA025149

Title:

Membrane Proteins of the Erythrocyte and their Arrangement as a Function of both 'in Vitro' and 'in Vivo' Aging.

Descriptive Note:

Annual progress rept. 1 Apr 75-31 Mar 76,

Corporate Author:

SAINT JUDE CHILDREN'S RESEARCH HOSPITAL MEMPHIS TENN

Personal Author(s):

Report Date:

1976-03-22

Pagination or Media Count:

5.0

Abstract:

The mechanisms by which the metabolic state of the erythrocyte influences lectin agglutinabilities has been investigated. Our results provide evidence for 1 a role of ATP in modulating PHA-P agglutinability. On the other hand, with Con A there is a complete lack of influence of ATP on agglutination 2 involvement of the transfer of the gamma-P of ATP in the modulation of PHA-P agglutinability 3 an ATP-induced surface charge decrease as reflected by aqueous polymer two-phase partitioning with ATP-induced PHA-P which can be correlated with increased agglutinability of the cell 4 the possibility that the same ATP-mediate molecular event which underlies the PHA-P agglutinability increase may also govern ATP-sensitive morphological transitions of the erythrocyte 5 specificity and ready reversibility of the adenosine effect on Con A agglutinability and 6 the elucidation of interactions of glyceraldehyde-3-phosphate dehydrogenase GAPD and of the glucose transport carrier, both adenosine-sensitive, with the Con A agglutinating system. Finally, during the past year, improved methods for the separation of membrane proteins into molecular weight classes has been developed using discontinuous buffer systems.

Subject Categories:

  • Medicine and Medical Research

Distribution Statement:

APPROVED FOR PUBLIC RELEASE