Jul 8, 1976

Human pancreatic-type ribonucleases with activity against double-stranded ribonucleic acids

Biochimica Et Biophysica Acta
A BardońD Shugar

Abstract

Purified acid-thermostable ribonuclease (Ribonucleate 3'-pyrimidino-oligonucleotidohydrolase, EC 3.1.4.22) from human pancreas degrades double-stranded RNA at 2% the rate for single-stranded RNA. The activities against single-stranded RNA and double-stranded RNA were shown to be due to a single enzyme with properties similar to bovine pancreatic RNAase A. For purposes of comparison the activities against double-stranded RNA of crystalline ribonucleases of the whale, rat and cow were assayed and found to be 0.4%, 0.03% and 0.003%, respectively, of their activities against single-stranded RNA. Both human serum and urine contain RNAse components of pancreatic origin which hydrolyze double-stranded RNA at 2% and 0.4%, respectively, of the rates against single-stranded RNA. By contrast, purified acid-thermostable RNAases from human spleen and liver hydrlyze double-stranded RNA at least 20-fold more slowly than human pancreatic RNAase, relative to the corresponding rates against single-stranded RNA. The human pancreatic and serum enzymes exhibit appreciable activity against the poly(C) component of the double-stranded poly(I)-poly(C); they also attack poly(C) itself at approximately 25 times the rate for poly(U) and at more than 50 t...Continue Reading

  • References15
  • Citations13

References

Mentioned in this Paper

Urine
Enzymes, antithrombotic
Spleen
Structure-Activity Relationship
RNA, Double-Stranded
Tissue Specificity
Benign Tumor of Pancreas
Bos taurus
Alkaline Ribonuclease
Enzymes for Treatment of Wounds and Ulcers

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