PMID: 4516197Jul 1, 1973

Purification and properties of ribonuclease H of calf thymus

Proceedings of the National Academy of Sciences of the United States of America
J G Stavrianopoulos, E Chargaff

Abstract

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, and Mn are described. It is inhibited by S-adenosylmethionine. The substrates cleaved were poly(dT).poly(rA) and the DNA-RNA hybrid made from phage f1 DNA; ribosomal RNA was not attacked.

References

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Citations

Jun 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·W Keller
Nov 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·W Keller, R Crouch
Jul 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·J G StavrianopoulosE Chargaff
Sep 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·J G StavrianopoulosE Chargaff
Aug 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·J D Karkas
Feb 1, 1972·Proceedings of the National Academy of Sciences of the United States of America·J D KarkasE Chargaff
Sep 1, 1971·Proceedings of the National Academy of Sciences of the United States of America·J G StavrianopoulosE Chargaff
Mar 16, 1964·Biochimica Et Biophysica Acta·A POLSONF J JOUBERT

Related Concepts

Manganese
Structure of Calf of Leg
Neoplasm of Uncertain or Unknown Behavior of Thymus
SDS-PAGE
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Chromatography, DEAE-Cellulose
Polynucleotides
Gumbaral

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