Extraction and Purification of Radioprotective Substance 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...
متن کاملPurification and properties of thymidylate synthetase from calf thymus.
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 of RNA polymerase IIO from calf thymus.
Three subspecies of RNA polymerase II, designated IIO, IIA, and IIB, have been described in calf thymus and shown to differ in the apparent molecular weight of their largest subunits, designated IIo, IIa, and IIb, respectively. The objective of this study was to develop a procedure for the purification of RNA polymerase IIO. This form of the enzyme predominates in vivo and is responsible for th...
متن کاملPurification and properties of ribonuclease H of calf thymus.
Ribonuclease H of calf thymus has been purified better than 3000-fold to yield an almost homogeneous preparation. The enzyme, which comprises about 0.03% of the total protein in the initial extract, is a slightly acidic protein (pI = 4.95) of molecular weight of about 64,000, possibly composed of subunits. The enzyme requires a metal ion for activation; the conditions for activation by Mg, Co, ...
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ژورنال
عنوان ژورنال: Journal of Radiation Research
سال: 1971
ISSN: 0449-3060,1349-9157
DOI: 10.1269/jrr.12.105