Multiple forms of fructose diphosphate aldolase in mammalian tissues.
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چکیده
منابع مشابه
Isolation 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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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 کاملRapid cessation of phospholipid synthesis in fructose-1,6-diphosphate aldolase mutants of Escherichia coli.
Escherichia coli GH352, which was originally described as a temperature-sensitive strain containing a thermolabile acyl coenzyme A:monoacylglycerol 3-phosphate acyltransferase, does not now contain a thermolabile form of this enzyme. It has a defect in fructose-1,6-diphosphate aldolase and at least one additional temperature-sensitive lesion. Both strains GH352 and NP315, a temperature-sensitiv...
متن کاملPhenotypic suppression of a fructose-1,6-diphosphate aldolase mutation in Escherichia coli.
Strain NP 315 of Escherichia coli possesses a thermolabile fructose-1, 6-diphosphate (FDP) aldolase; its growth on carbohydrate substrates is inhibited probably as a consequence of the accumulation of high intracellular levels of FDP. Studies of one class of phenotypic revertants of strain NP 315 which have regained their ability to grow on C(6) substrates at 40 C showed that in these strains t...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1966
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.56.4.1275