Iodination of Muscle Fructose Diphosphate Aldolase
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چکیده
منابع مشابه
Inhibition of fructose diphosphate aldolase by phosphatidylserine liposomes.
Phosphatides and their cleavage products modulate the activities of a variety of proteins, including glycolytic enzymes. Very abundant glycolytic enzyme fructose bis-phosphate aldolase was found to be strongly inhibited by phosphatidylinositol (PI) in the form of liposomes, which was interpreted as a result of electrostatic interaction of the protein with t h e negatively charged liposomes (Gut...
متن کاملRegulation of fructose diphosphate aldolase concentrations in skeletal muscles of normal and dystrophic chickens.
We are using the glycolytic enzyme aldolase as a marker to investigate the molecular basis for reduced levels of specific enzyme activities associated with muscular dystrophy. Inbred strains of normal and dystrophic chickens were used as models to study the disease. In the present paper we show that: 1) aldolase & was the only isoenzyme present in normal and dystrophic muscles derived from lto ...
متن کاملProperties of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase.
Böck, August (Purdue University, Lafayette, Ind.), and Frederick C. Neidhardt. Properties of a mutant of Escherichia coli with a temperature-sensitive fructose-1,6-diphosphate aldolase. J. Bacteriol. 92:470-476. 1966.-A mutant of Escherichia coli in which fructose-1,6-diphosphate aldolase functions at 30 C but not at 40 C was used to study the physiological effect of a specific block in the Emb...
متن کاملIsolation of a Mutant of Escherichia coli with a Temperature-sensitive Fructose-1,6-Diphosphate Aldolase Activity.
Böck, August (Purdue University, Lafayette, Ind.), and Frederick C. Neidhardt. Isolation of a mutant of Escherichia coli with a temperature-sensitive fructose-1,6-diphosphate aldolase activity. J. Bacteriol. 92:464-469. 1966.-A mutant of Escherichia coli was isolated which was able to grow in rich medium at 30 C but not at 40 C. Upon exposure to 40 C, the cells immediately stopped ribonucleic a...
متن کاملIsolation and characterization of the cytosolic and chloroplast forms of spinach leaf fructose diphosphate aldolase.
Two different isoenzymes of fructose-P2 aldolase can be resolved by chromatography of crude spinach leaf extracts on DEAE-cellulose columns. The acidic isoenzyme comprises about 85% of the total leaf aldolase activity. The two forms differ in primary structure as judged by their distinctive amino acid compositions, tryptic peptide patterns, and immunological properties. Only the acidic isoenzym...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)81725-8