Accession Number : AD0458593

Title :   PROTEIN ALTERATIONS IN ERYTHROCYTES AT LOW TEMPERATURES.

Descriptive Note : Final rept., 1 Mar 63-28 Feb 65,

Corporate Author : BJORKSTEN RESEARCH LAB INC MADISON WI

Personal Author(s) : Bjorksten, J. ; Andrews, F. A. ; Ashman, S. M. ; Poole, Rosalind

Report Date : 28 FEB 1965

Pagination or Media Count : 11

Abstract : Human red cells were frozen-thawed and studied for alterations of cellular proteins. Through the use of microincineration it was found that intracellular minerals were displaced centrally in frozen-thawed cells. The resulting shift in ionic strength from one part of the cell to another could adversely affect proteins, thereby reducing viability of frozen-thawed cells. A hemoglobin-containing complex was discovered which was cold labile, in contradistinction to hemoglobin itself. Alterations in stroma proteins were studied using protein fractionation techniques. In general it was found that less total nitrogen was extracted from stroma which had been frozen-thawed. Acetylcholinesterase activity in stroma extracts derived from frozenthawed cells, however, was much higher than the activity of stroma from the unfrozen counterpart. General cellular respiration studies using Warburg techniques and also specific assays for glucose-6-phosphate dehydrogenase indicated that low temperature treatment of red cells does not alter carbohydrate-oxidizing enzyme systems. It is concluded that low temperature storage causes minimal biochemical damage to red cells, but does result in depolymerization of biological complexes within the cells, which may well be a cause of the shortened normal life span of red cells in circulation. (Author)

Descriptors :   (*ERYTHROCYTES, FREEZING), (*CYTOCHEMISTRY, ERYTHROCYTES), MOLECULAR PROPERTIES, TISSUE EXTRACTS, LOW TEMPERATURE, ACETYLCHOLINESTERASE, BIOCHEMISTRY, NITROGEN, POLYMERIZATION, PROTEINS, HEMOGLOBIN, IONS, CHEMICAL ANALYSIS, PRESERVATION, VIABILITY, HEAT TREATMENT.

Distribution Statement : APPROVED FOR PUBLIC RELEASE