Centrifugal analysis of undiluted packed human erythrocyte lysates studies of the association of glyceraldehyde-phosphate dehydrogenase with the membrane fraction

doi:10.1016/0304-4165(83)90301-X

Biochimica et Biophysica Acta (BBA) - General Subjects

Volume 758, Issue 2, 29 July 1983, Pages 187-190

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Abstract

Concentrated human erythroyte lysates (greater than 99% initial haematocrit) were subjected to high centrifugal fields. This caused the membrane fraction to separate from the cytoplasmic portion, due to the lower density of the former. Enzyme distribution data indicated that glyceraldehyde-phosphate dehydrogenase was predominantly in the cytoplasmic fraction.

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This chapter presents the interactions of glycolytic enzymes with cellular membranes. It is generally accepted that glycolytic enzymes are located in the cytoplasm or extramitochondrial regions of mammalian cells. However, there is at present ample evidence that some of these enzymes are associated with macromolecules of the cells. Mammalian hexokinase activity is partitioned between particulate and soluble fractions. In brain homogenates, as much as 80% of the enzyme is found in the mitochondrial fractions, and in other tissues a considerable proportion of the enzyme is also in particulate rather than soluble fractions. Cellular location of hexokinase may differ depending on the tissues or cell types. This is related perhaps to the physiological importance of the enzyme and of glycolysis in the overall metabolism of glucose in these cells. The protection against degradation may be crucial for the survival of red cells as these anucleated cells lack the capacity to synthesize the enzymes. Another possibility is that drastic conditions, such as ischemia, demanding rapid activation of glycolysis may require participation of the membrane-bound enzymes such as hexokinase and PFK, both more active forms than the free enzymes.
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BBA reportCentrifugal analysis of undiluted packed human erythrocyte lysates studies of the association of glyceraldehyde-phosphate dehydrogenase with the membrane fraction

Abstract

Curr. Top. Cell. Regul.

J. Biol. Chem.

J. Biol. Chem.

FEBS Lett.

J. Biol. Chem.

Biochim. Biophys. Acta

Biochem. J.

Biochem. J.

BBA report
Centrifugal analysis of undiluted packed human erythrocyte lysates studies of the association of glyceraldehyde-phosphate dehydrogenase with the membrane fraction