Purification of Deoxyribonucleohistone from Wheat Germ
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چکیده
منابع مشابه
Methionine-tRNA-ligase from wheat germ: purification and properties.
Methionine-t RNA-ligase (AMP) EC 6.1.1.10, from various prokaryotic organisms has been extensively studied since it has been found to catalyse the aminoacylation of tRNAsMef, thus contributing to the incorporation of methionine at both initiation and elongation steps of protein chains synthesis. Similarly, two different eukaryotic tRNAsMet, especially in plant cytoplasm are required for methion...
متن کاملPurification and characterization of a wheat germ protein kinase.
A cyclic AMP-independent protein kinase has been purified from wheat germ extracts. The enzyme catalyzes the phosphorylation of casein and phosvitin but not protamine, histone, or bovine serum albumin. However, the best substrate for the kinase appears to be that of an endogenous wheat germ protein. The kinase can utilize both ATP and GTP as phosphoryl donors. A molecular weight of 36,000-38,00...
متن کاملThe purification and characterization of wheat-germ agglutinin.
The purification of wheat-germ agglutinin by precipitation with ammonium sulphate and by chromatography on Sephadex G-75, Sepharose-ovomucoid and CM-cellulose is described. This procedure gave agglutinin preparations which were homogeneous on polyacrylamide gels under a variety of conditions. Purified wheat-germ agglutinin formed colourless solutions and was relatively insoluble at neutral pH; ...
متن کاملPurification and properties of guanine, queuine-tRNA transglycosylase from wheat germ.
Guanine, queuine-tRNA transglycosylase has been purified from wheat germ to homogeneity. The specific activity is 2,000 pmol h-1 mg-1 of protein. The enzyme has an apparent Mr = 140,000. It migrates as a single band with Mr = 68,000 on electrophoresis in sodium dodecyl sulfate gels, indicating two Mr = 68,000 subunits. Both guanine (Km = 6.0 X 10(-8) M) and queuine (KI = 9.5 X 10(-8) M) are sub...
متن کاملPurification and properties of a high specific activity protein kinase from wheat germ.
A protein kinase was extensively purified to near-homogeneity from wheat germ by a procedure involving affinity chromatography on casein-Sepharose 4B, gel filtration, and repeated chromatography on carboxymethyl-Sepharose CL-6B. The protein kinase preparations have the highest specific activities (up to 656 nanomoles phosphate incorporated per minute per milligram of protein) yet reported for p...
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ژورنال
عنوان ژورنال: Nippon kagaku zassi
سال: 1957
ISSN: 0369-5387,2185-0917
DOI: 10.1246/nikkashi1948.78.1058