Protection of succinic dehydrogenase thiol groups by fluoride and phosphate
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چکیده
منابع مشابه
Coenzyme binding and the thiol groups of glyceraldehyde-3-phosphate dehydrogenase.
Glyceraldehyde-3-phosphate dehydrogenase is inhibited by iodoacetate and under certain conditions it is activated by cysteine and reduced glutathione (1,2). It has therefore been concluded that the enzyme contains thiol groups which are essential for its activity. A relationship between the thiol groups of the enzyme and diphosphopyridine nucleotide (DPN) was first suggested by Rapkine, Rapkine...
متن کاملComparison of response of succinic dehydrogenase and succinoxidase system to organic mercurial and thiol compounds.
Our earlier observations (l), extended in the present report, had indicated that the aerobic succinoxidase system was more sensitive to phenyhnercuric nitrate than the anaerobic succinic dehydrogenase system. Slater in a preliminary communication (2) called attention to a similar difference in sensitivity to p-chloromercuribenzoic acid. In studies of protection against mercurial inhibition by t...
متن کاملInhibition of succinic dehydrogenase by oxalacetate.
Although the inhibition of succinic dehydrogenase by oxalacetate is a generally accepted fact, there is a paucity of data on the subject. In 1937 Das (l), using a modified Thunberg technique, reported that the enzyme was 50 per cent inhibited by 2 X 1O-5 M oxalacetate when the succinate concentration was 0.025 M. In 1939 Potter (2) reported that the oxidation of succinate by liver and kidney ho...
متن کاملInhibition of succinic dehydrogenase by methylglyoxal.
The reaction of the carbonyl group of methylglyoxal with -SH radicals of thiols has been the subject of numerous investigations (l-9). The reactivity of the keto aldehyde with -SH compounds suggested that a similar type of reaction may occur between methylglyoxal and -SH proteins. The physiological r&e of methylglyoxal as an inhibitor of -SK enzymes is of particular interest, since this keto al...
متن کاملRole of the essential thiol groups of yeast alcohol dehydrogenase.
1. Yeast alcohol dehydrogenase inactivated by reaction with iodoacetamide retains 85% of the original NADH-binding capacity as measured under conditions of saturating coenzyme concentration. 2. The dissociation constant of the enzyme-NADH complex is unaffected by inactivation of the enzyme with iodoacetamide, and the affinity of the enzyme for NAD(+) and pyridine-3-aldehyde-adenine dinucleotide...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1956
ISSN: 0306-3283
DOI: 10.1042/bj0640196