Purification and properties of muscle phosphoglycerate kinase.
نویسندگان
چکیده
powder; cold-acid hydrolysed; hot-acid hydrolysed. In addition there was a significant quantity of metabolites remaining water-soluble after all forms of hydrolysis. 4. When 1 or 2 hr. fractions of bile were analysed the proportion of radioactivity excreted as glucuronide always decreased in successive samples, whereas water-soluble metabolites generally increased. In some animals the proportion of coldacid-hydrolysed metabolites increased and in others decreased. No consistent change was detectable in hot-acid-hydrolysed radioactivity. A similar trend was seen in successive urine samples. 5. The relationship of these results to similar studies of progesterone in man and other animals is discussed.
منابع مشابه
Altered phosphoglycerate kinase in aging rats.
Pure phosphoglycerate kinase from young and old rat muscle shows substantial differences in properties. Compared to the "young" enzyme, phosphoglycerate kinase isolated from old animals possesses a greater stability to heat and storage, a slower reacting -SH group, an altered UV spectrum, and requires more antiserum prepared to "young" enzyme for 50% inactivation. Km and specific activity are u...
متن کاملBiochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins.
The glycolytic enzyme enolase (EC 4.2.1.11) is active as dimers formed from three subunits encoded by different genes. The embryonic alphaalpha isoform remains distributed in many adult cell types, whereas a transition towards betabeta and gammagamma isoforms occurs in striated muscle cells and neurons respectively. It is not understood why enolase exhibits tissue-specific isoforms with very cl...
متن کاملSeparation, purification, and comparative properties of chloroplast and cytoplasmic phosphoglycerate kinase from barley leaves.
The chloroplast and cytoplasmic isoenzymes of phosphoglycerate kinase (PGK) (EC. 2.7.2.3) from Hordeum vulgare leaves have been separated and purified for the first time to apparent homogeneity. The method for purifying the isoenzymes is described here and consists of DEAE Sephacel chromatography followed by affinity chromatography on ATP Sepharose. This consistently provided a 500- to 900-fold...
متن کاملCrystalline 3-phosphoglycerate kinase from skeletal muscle.
1. A procedure for preparing crystalline 3-phosphoglycerate kinase from rabbit or pig skeletal muscle is presented. 2. The preparation phosphorylates up to 975mumoles of 3-phosphoglycerate/min./mg. at 30 degrees and is not contaminated with myokinase. 3. The enzyme has an estimated molecular weight of 36500+/-1000, and contains three residues each of tyrosine and tryptophan. 4. The preparation ...
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...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Biochemical journal
دوره 81 شماره
صفحات -
تاریخ انتشار 1961