منابع مشابه
Partial purification of mitochondrial RNA polymerase from rat liver.
Mitochondrial RNA polymerase activity from rat liver has previously been demonstrated in intact organelles. This activity has now been solubilized, partially purified, and shown to be a true polymerase, free of nuclease. The enzyme is derived from mitochondria and is not from contaminating bacteria or nuclear components. The enzyme is distinguished from its nuclear counterparts by its behavior ...
متن کاملPartial purification of detergent-soluble HL-A antigen and its cleavage by papain.
HL-A antigen solubilized with the non-ionic detergent, Brij 99, has been purified to about 50% of homogeneity from a cultured human lymphoblast line. It consists of two nonidentical subunits of 44,000 and 12,000 molecular weight (MW). Upon papain proteolysis the 44,000 MW peptide is converted by at least two cleavages to a 34,000 MW peptide, but the 12,000 MW peptide appears to be unchanged. Co...
متن کاملPartial purification and kinetic properties of a soluble estrogen glucuronyltransferase from pig intestine.
A soluble enzyme from the small intestine of the pig, capable of conjugating uridine diphosphate glucuronic acid with 17/3-estradiol, has been purified 5to IO-fold. The glucuronide formed was identified as 17P-estradiol J-monoglucuronide by paper chromatography and microchemical reactions. This estrogen glucuronyltransferase is present in the 150,000 x g supernatant and shows an absolute requir...
متن کاملPartial Purification and Preliminary Characterization of Soluble Leaf Proteins Specific to Virus Infected Tobacco Plants
The' b' protein components specific to virus infected tobacco leaves (Gianinazzi, Martin & Vall~e, 197o) can be partially purified by preferential extraction at pH 2.8. Evidence is presented that they are rich in aromatic amino acids. Results of treatment of the proteins with SDS and subsequent separation by gel electrophoresis in the presence of SDS suggest that b~, b~ and b~ are composed of t...
متن کاملPreparation and partial purification of soluble choline dehydrogenase from liver mitochondria.
Choline dehydrogenase is the initial enzyme of the complete choline oxidase system. The latter includes all agents and enzymes involved in hydrogen transport to oxygen plus the initial dehydrogenase. Problems concerning the properties of choline dehydrogenase have remained unsolved largely because of the insoluble nature of the enzyme. It has resisted solution by such techniques as freezing and...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1960
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.46.6.811