Phosphorylation and activation of poly(A)-endoribonuclease from calf thymus gland
نویسندگان
چکیده
منابع مشابه
Deoxynucleotide-polymerizing Enzymes of Calf Thymus Gland
Replication of polydeoxyadenylate and polydeoxythymidylate catalyzed by the high molecular weight DNA polymerase proceeds only in the presence of a complementary oligodeoxynucleotide. The oligodeoxynucleotide initiator chain must be greater than 6 nucleotides for poly(dA) replication and greater than 5 nucleotides for poly(dT) replication. The initiator oligonucleotide is incorporated into prod...
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 کاملGlutaredoxin 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 کاملDeoxycytidine kinase from calf thymus.
Kinetic constants were determined for 34 nucleoside substrates of deoxycytidine kinase (EC 2.7.1.74) from calf thymus. Substrate efficiency was assessed by the ratio of V,,,,. to K,. Inhibition constants were determined for 61 nonsubstrate nucleosides or nucleoside analogues. The enzyme was relatively specific for the pentose moiety of nucleoside substrates. P-D-2’-Deoxyribonucleosides were mor...
متن کاملRole of actin and tubulin in the regulation of poly(A) polymerase-endoribonuclease IV complex from calf thymus.
The poly(A) polymerase from calf thymus (Mr = 62,000) is associated with the poly(A)-specific endoribonuclease IV (Mr = 45,000); this complex is dissociable at pH 8.2. The activities of the two enzymes in the complex are strongly inhibited by the G-actin and tubulin (both in the subunit-dissociated and in the polymeric form); F-actin was less inhibitory, while myosin and actomyosin were without...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1982
ISSN: 0014-5793
DOI: 10.1016/0014-5793(82)80897-1