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Enzyme activities of cultured erythroblasts
Author(s) -
Shinohara Kenji,
Yamada Katsunori,
Inoue Masamitsu,
Yoshizaki Yoshiki,
Ishida Yoji,
Kaneko Toshio,
Matsumoto Noboru
Publication year - 1985
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.2830200207
Subject(s) - enzyme , medicine , chemistry , biochemistry
The enzyme activities of cultured early erythroid progenitor cells (burst‐forming unit erythroid, BFU‐E) were measured and were compared with the activities of mature erythrocytes. The enzyme activity of acetylcholinesterase was not detectable in the erythroblasts. The ratios of phosphofructokinase and glutathione peroxidase were low due to low enzyme activities in both the erythroblasts and erythrocytes. The ratios of triose phosphate isomerase, phosphoglycerate kinase, and adenylate kinase were low due to high enzyme activities in both the erythroblasts and erythrocytes. The ratios of hexokinase, glucose phosphate isomerase, monophosphoglyceromutase, pyruvate kinase, and adenosine deaminase were high due to high enzyme activities in the erythroblasts. The isozyme of erythroblast hexokinase was of the prototype isozyme I, while pyruvate kinase was predominantly of the prototype M 2 , with two hybrid isozymes to the anodal side by electrophoresis. These facts suggest that there is a greatly different metabolic pattern during the maturation of the erythroid cells.