Deoxynucleotide-polymerizing Enzymes of Calf Thymus Gland

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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...

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Deoxynucleotide-polymerizing enzymes of calf thymus gland. II. Properties of the terminal deoxynucleotidyltransferase.

and the ratio of polymer nucleotide to monomer at equilibrium (pH 7.0, 35’) is about 99 when X and Y = adenine. Puriue deoxyribonucleoside triphosphate polymerizations proceed readily in 8 mM Mgf+ at low buffer strengths (40 mr+r). For deoxyadenosine triphosphate, under these conditions, K, = 1.1 x 10-‘&r and I’,,, varies from about 0.03 to 0.30 pmole mm+ mg+ with various oligodeoxynucleotide i...

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Doxynucleotide-polymerizing enzymes of calf thymus gland. IV. Inhibition of terminal deoxynucleotidyl transferase by metal ligands.

The polymerization of deoxynucleoside triphosphates, catalyzed by terminal deoxynucleotidyl transferase from calf thymus gland, is strongly inhibited by various metal chelators. The reaction appears to be first order with respect to enzyme, deoxynucleoside triphosphate, and initiator, indicating that there is only one catalytic center for each enzyme molecule. The presence of metal chelator doe...

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Deoxynucleotide-polymerizing enzymes in normal and malignant human cells.

The cytoplasmic (175,000 x g supernatant) and the chromatin fractions from phytohemagglutinin-stimulated normal human lymphocytes, human thymus tissue, lympho cytes from chronic lymphocytic leukemia and acute lymphoblastic leukemia patients and cultured cells of normal (RPMI 1788), multiple myeloma (RPMI 8226), Burkitt lymphoma (HR1K), and acute lymphoblastic leukemia (Molt-4) origin were exami...

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Purification 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...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1971

ISSN: 0021-9258

DOI: 10.1016/s0021-9258(18)62410-x