Purification and Substrate Specificity of Yeast Isoamylase
نویسندگان
چکیده
منابع مشابه
The glycosylceramidase in the murine intestine. Purification and substrate specificity.
The intestinal glycosylceramidase of the mouse which we reported previously as a taurodeoxycholate-activated galactosylceramidase (Kobayashi, T., and Suzuki, K. (1981) J. Biol. Chem. 256, 1133-1137) has been purified to homogeneity. The enzyme gave a single band of a molecular weight of 130,000 in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The molecular weight estimated by S...
متن کاملSubstrate specificity of fatty acid synthetase from yeast.
The purified multienzyme complex fatty acid synthetase from yeast synthesizes palmitoyland stearoyl-CoA with NADPH, ace@-CoA and malonylCoA as substrates. At least seven different enzymatic steps have been shown to occur in the overall synthesis by the use of appropriate model substrates [l] , .e.g. S-acetoacetyl-N-acetylcysteamine for the @-ketoreductase partial activity. As reported in this c...
متن کاملPartial purification and substrate specificity of a ubiquitin hydrolase from Saccharomyces cerevisiae.
A ubiquitin hydrolase that removes ubiquitin from a multi-ubiquitinated protein has been purified 600-fold from Saccharomyces cerevisiae. Four different ubiquitin-protein conjugates were assayed as substrates during the purification procedure. Enzymic activities that removed ubiquitin from ubiquitinated histone H2A, a ubiquitin-ubiquitin dimer and a ubiquitin-ribosomal fusion protein were separ...
متن کاملPurification and substrate specificity of pyrimidine nucleoside phosphorylase from Haemophilus influenzae.
A single pyrimidine nucleoside phosphorylase was found to comprise both uridine phosphorylase and thymidine phosphorylase activities in Haemophilus infiuenzae. The enzyme has been purified 400-fold, and was stabilized by dithiothreitol and glycerol. Evidence that a single enzyme cleaves both ribonucleosides and deoxynucleosides was obtained from gel electrophoresis, heat inactivation studies, a...
متن کاملPurification, characterization and substrate specificity of calmodulin-dependent myosin light-chain kinase from bovine brain.
A substrate-specific calmodulin-dependent myosin light-chain kinase (MLCK) was purified 45,000-fold to near homogeneity from bovine brain in 12% yield. Bovine brain MLCK phosphorylates a serine residue in the isolated turkey gizzard myosin light chain (MLC), with a specific activity of 1.8 mumol/min per mg of enzyme. The regulatory MLC present in intact gizzard myosin is also phosphorylated by ...
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: Agricultural and Biological Chemistry
سال: 1969
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.33.1535