Aug 1, 1980

The ribonucleases of bovine skeletal muscle

The Biochemical Journal
G E DaviesC C Levy

Abstract

Bovine skeletal muscle contains small amounts of at least six heat- and acid-stable RNA-degrading enzymes. Our results are the first evidence for multiple ribonucleases in skeletal muscle. Three of these have been highly purified, and each has been shown to be a pyrimidine-specific endoribonuclease by use of a rapid sequencing technique employing gel electrophoresis. However, synthetic co-polymers containing adenylate or guanylate residues in addition to pyrimidine residues are hydrolysed at higher rates than are the pyrimidine homopolymers. With 0.63 mM yeast RNA as substrate, all three enzymes (ribonucleases I, II and III) are optimally active in alkaline solution (pH 7.5-8.5) containing 0.05-0.15 M univalent salts, do not require bivalent cations, and have molecular weights of 13 000-20 000. The properties of muscle ribonuclease I are very similar to those of bovine pancreatic ribonuclease A. Muscle ribonucleases II and III have characteristics similar to those of ribonucleases found in various other bovine tissues. In common with all previously studied pyrimidine-specific endoribonucleases, the bovine muscle ribonucleases are inhibited by such purine homopolynucleotides as polyadenylate. Furthermore, polyamines, present in ...Continue Reading

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Mentioned in this Paper

Cations, Divalent
Enzymes, antithrombotic
Bos taurus
Polynucleotides
Poly A
Alkaline Ribonuclease
Sequencing
Cations
Polymers
Enzymes for Treatment of Wounds and Ulcers

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