Purification and properties of human cataractous lens glyceraldehyde-3-phosphate dehydrogenase
作者:
JedziniakJudith,
MeysMichael,
ArredondoLuz Marina,
期刊:
Current Eye Research
(Taylor Available online 1985)
卷期:
Volume 4,
issue 7
页码: 747-752
ISSN:0271-3683
年代: 1985
DOI:10.3109/02713688509020029
出版商: Taylor&Francis
数据来源: Taylor
摘要:
Glyceraldehyde-3-phosphate dehydrogenase has been shown to occur in three different forms in the human adult cataractous lens: a membrane bound form (M) and at least two cytosolic isozymes: I1and I2. Similar Km's for substrate, cofactor and HAsO4, were established for each form and all three forms, to differing degree, require a reduced sulfhydryl group for maximum activity. A variety of phosphonucleosides (ATP, ADP, AMP and 3′5′cyclic AMP) as well as NADH inhibit enzyme activity. Inhibition by ATP is non-competitive whereas cyclic AMP and NADH compete for the cofactor binding site. Chloride ion stimulates and inhibits enzyme activity at low and high concentrations respectively.
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