Membrane Proteins of the Erythrocyte and their Arrangement as a Function of both 'in Vitro' and 'in Vivo' Aging.
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.
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 22, 1976
- Accession Number
- ADA025149
Entities
People
- Martin Morrison