Purification, Chemical Structure and Antitumor Activity of Octadecenoic Acid from Calf Thymus
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چکیده
منابع مشابه
Glutaredoxin from Calf Thymus PURIFICATION
The protein glutaredoxin, required for GSH-dependent ribonucleotide reduction, has been purified to homogeneity from calf thymus. The preparative method consisted of ammonium sulfate precipitation and three chromatography steps on DEAEkellulose, Sephadex G-50, and CM-Sepharose. Calf thymus glutaredoxin was assayed on the basis of its inherent GSH-disulfide transhydrogenase activity. Glutaredoxi...
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The enzyme, thymidylate synthetase, catalyzes the methylation of deosyuridylate to thymidylate, with formaldehyde as the source of the methyl group, in the presence of tetrahydrofolate. Some of the properties of this enzyme system in crude soluble protein extracts of rat thymus have previously been reported (1). Reports have also appeared of this enzyme reaction in Escherichia cozi (2, 3). The ...
متن کاملPurification of terminal riboadenylate transferase from calf thymus gland.
A poly(A) polymerase has been purified from the soluble protein fraction of calf thymus gland. The activity is cytoplasmic and nonparticulate. Mn-2+ATP is the preferred substrate. On the basis of disc gel electrophoresis in sodium dodecyl sulfate-acrylamide gels, gel filtration, and sedimentation velocity in sucrose gradients, the enzyme has a molecular weight of 62,000 and appears to consist o...
متن کاملPurification and amino-terminal amino acid sequence of an apurinic/apyrimidinic endonuclease from calf thymus.
An apurinic/apyrimidinic (AP) endonuclease (E.C.3.1.25.2) has been purified 1100 fold to apparent homogeneity from calf thymus by a series of ion exchange, gel filtration and hydrophobic interaction chromatographies. The purified AP endonuclease is a monomeric protein with an apparent molecular weight on SDS-PAGE of 37,000. On gel filtration the protein behaves as a protein of apparent molecula...
متن کاملPurification and physical characterization of nucleic acid helix-unwinding proteins from calf thymus.
We have devised a general protein fractionation procedure which selects for eukaryotic DNA-binding proteins, some of which resemble DNA-unwinding proteins from prokaryotes. Proteins were selected which (a) pass through a native DNA-cellulose column, (b) bind to a denatured DNA-cellulose column, and (c) remain bound to the latter column during a rinse with a dilute solution of the sodium salt of...
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ژورنال
عنوان ژورنال: Journal of Japan Oil Chemists' Society
سال: 1972
ISSN: 1884-2003
DOI: 10.5650/jos1956.21.846