Open AccessAssociation of Glyceraldehyde‐3‐Phosphate Dehydrogenase with the Particulate Fraction of Chicken Skeletal Muscle
Author(s) -
DAGHER Shawky M.,
HULTIN Herbert O.
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb02150.x
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , ionic strength , dehydrogenase , enzyme , chemistry , fraction (chemistry) , biochemistry , phosphate , glyceraldehyde , chromatography , enzyme assay , particulates , organic chemistry , aqueous solution
When chicken breast muscle was homogenized in water, approximately 86% of the glyceraldehyde‐3‐phosphate dehydrogenase was associated with the particulate fraction. The enzyme was solubilized by increasing pH with a very marked increase in the pH range of 6.9 to 7.1. At low ionic strength (about 0.015), approximately 50% of the enzyme is solubilized at pH 7.5 and above. Increasing ionic strength also led to increased solubilization. In addition, there was a specific cation effect with Ca 2+ > Mg 2+ > K + > Na + at a constant ionic strength. Glyceraldehyde 3‐phosphate and 2,3‐bisphosphoglycerate were effective in partially solubilizing the enzyme. Solubilized glyceraldehyde‐3‐phosphate dehydrogenase can rebind to the particulate fraction of the homogenized muscle. The soluble form of the enzyme has a higher V and a higher K m (glyceraldehyde 3‐phosphate) than the enzyme bound to the particulate fraction.