Cell-free synthesis of fructose diphosphate aldolases A, B, and C.
نویسندگان
چکیده
منابع مشابه
Purification and characterization of two fructose diphosphate aldolases from Escherichia coli (Crookes' strain).
Two fructose diphosphate aldolases (EC 4.1.2.13) were detected in extracts of Escherichia coli (Crookes' strain) grown on pyruvate or lactate. The two enzymes can be resolved by chromatography on DEAE-cellulose at pH7.5, or by gel filtration on Sephadex G-200, and both have been obtained in a pure state. One is a typical bacterial aldolase (class II) in that it is strongly inhibited by metal-ch...
متن کاملProperties of fructose 1,6-diphosphate aldolases from spores and vegetative cells of Bacillus cereus.
Fructose 1,6-diphosphate aldolase from cells of Bacillus cereus appears to be typical Class II aldolase as judged by its functional and physical properties. Spore and vegetative cell aldolase had similar enzymatic, immunochemical, and heat resistance properties in the absence of calcium, but they differed in their thermal stabilities in the presence of calcium, their Stokes' radii, their mobili...
متن کاملProperties of Fructose 1,6-Diphosphate Aldolases from Spores and Vegetative Cells of Bacillus cereus1
Fructose 1,6-diphosphate aldolase from cells of Bacillus cereus appears to be typical Class II aldolase as judged by its functional and physical properties: Spore and vegetative cell aldolase had similar enzymatic, immunochemical, and heat resistance properties in the absence of calcium, but they differed in their thermal stabilities in the presence of calcium, their Stokes' radii, their mobili...
متن کاملInactivation of Class I Fructose Diphosphate Aldolases by the Substrate Analog N-Bromoacetylethanolamine
N-Bromoacetylethanolamine phosphate, prepared by the bromoacetylation of ethanolamine phosphate, has been tested as an active site-specilic reagent for rabbit and rat muscle fructose diphosphate aldolases. The reagent inactivates both enzymes, and inactivation is prevented by substrates or competitive inhibitors. Loss of activity is pseudo-first order until the later stages of inactivation, and...
متن کاملInactivation of class I fructose diphosphate aldolases by the substrate analog N-bromoacetylethanolamine phosphate.
N-Bromoacetylethanolamine phosphate, prepared by the bromoacetylation of ethanolamine phosphate, has been tested as an active site-specilic reagent for rabbit and rat muscle fructose diphosphate aldolases. The reagent inactivates both enzymes, and inactivation is prevented by substrates or competitive inhibitors. Loss of activity is pseudo-first order until the later stages of inactivation, and...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1979
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)50718-3