CHANGES IN HUMAN ERYTHROCYTE MEMBRANE PROTEINS DURING STORAGE.

Abstract

Fresh and 21-day old human blood samples were used to prepare fresh and out-dated stromas. Pooled fresh and outdated samples were solubilized by butanol or pyridine. These two protein fractions (fresh and outdated) produced different patterns on disc electrophoresis and column chromatography. Charge differences between fresh and outdated proteins were shown to be independent of the sialic acid content of the proteins. Conformational changes between fresh and outdated proteins were seen using 1-anilino-8-naphthalene sulfonate (ANS) as a fluorescent probe. Fresh samples showed greater fluorescent enhancement but less total ANS binding, and lower protein-ANS dissociation constants. These changes may cause a reduction in the strength, or integrity, of the erythrocyte membrane and be a limiting factor in the viability of the human red cell during in vitro storage. (Author)

Document Details

Document Type
Technical Report
Publication Date
Jan 09, 1970
Accession Number
AD0703181

Entities

People

  • Donald A. Cooper
  • Gerald L. Moore
  • Ross S. Antonoff
  • Stephen L. Robinson

Organizations

  • United States Army Medical Research Laboratory

Tags

DTIC Thesaurus Topics

  • Analytical Chemistry Techniques
  • Blood
  • Cells
  • Chemical Compounds
  • Chromatography
  • Column Chromatography
  • Dissociation
  • Electrophoresis
  • Erythrocytes
  • Membrane Proteins
  • Membranes
  • Naphthalenes
  • Organic Compounds
  • Proteins
  • Pyridines
  • Sialic Acids

Fields of Study

  • Biology

Readers

  • Environmental Engineering
  • Molecular and Cellular Biochemistry
  • Systems Analysis and Design