Anomeric Specificity of Phosphofructokinase from Rabbit Muscle
نویسندگان
چکیده
منابع مشابه
Purification and Some Properties of Rabbit Skeletal Muscle Phosphofructokinase.
In spite of an abundant literature (1-15) indicating that phosphofructokinasel plays a key role in the regulation of carbohydrate metabolism, few attempts have been made to purify the enzyme (4, 17, 18) since the subject of P-fructokinase was last reviewed (19). The apparent instability of the enzyme makes purification difficult, and a number of suggestions have been offered to explain this pro...
متن کاملRabbit liver phosphofructokinase. Comparison of some properties with those of muscle phosphofructokinase.
A relatively simple procedure was devised for the purification of phosphofructokinase from rabbit liver extracts. The enzyme was purified more than 2600-fold with a yield of close to 50%. Liver phosphofructokinase migrates faster on zone electrophoresis than rabbit skeletal muscle phosphofructokinase. It also differs from muscle enzyme in stability, molecular weight, and kinetic properties. The...
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The consistent application of phosphatase inhibitors and a novel final purification step using a connected series of DE-51, DE-52, and DE-53 anion-exchange chromatography columns facilitate the preparation of electrophoretically homogeneous subpopulations of rabbit muscle phosphofructokinase which differ in their catalytic properties and endogenous covalent phosphate content. A band of "high"-p...
متن کاملPhosphocreatine does not inhibit rabbit muscle phosphofructokinase or pyruvate kinase.
Certain phosphocreatine preparations contain a contaminant that inhibits phosphofructokinase and pyruvate kinase assays. The contaminant can be separated from phosphocreatine by anion exchange chromatography. After appropriate purification, phosphocreatine has no effect on phosphofructokinase or pyruvate kinase; thus, there is no evidence that it serves muscle as a regulator of these enzymes. A...
متن کاملRabbit Brain Phosphofructokinase
A procedure was developed for the purification of phosphofructokinase from rabbit brain extracts. The enzyme was purified more than loo-fold with a yield of greater than 50%. It was found to have the same distribution of multiple molecular forms as found in the total brain extract, including one molecular species that is different from the more extensively studied muscle (heart) and liver (eryt...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1974
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)42216-3