Mar 15, 1976

Purification and properties of human acid-thermostable ribonucleases, and diagnosis of childhood pancreatic fibrosis

Clinica Chimica Acta; International Journal of Clinical Chemistry
A BardonD Shugar


Acid-thermostable ribonucleases were isolated from human pancreas, duodenal contents, liver, spleen, serum and urine, and purified 15--1000-fold. The pH optima, ionic requirements, and some of the specificity requirements, of these enzymes were investigated. The isolated enzymes formed two distinct groups: (a) The ribonucleases of the pancreas, duodenal contents and fraction A of serum and urine exhibit a pH optimum of 8.5, are inhibited by An2+ and Cu2+, and relatively rapidly hydrolyze the synthetic substrate uridine 3'-(alpha-naphthylphosphate); (b) the ribonucleases of the liver and spleen, and of fractions B of the serum and urine, with a pH optimum of 7, are less sensitive to An2+ and Cu2+, and exhibit negligible activity versus uridine 3'-(alpha-naphthylphosphate). Determination of the serum level of pancreatic-type ribonuclease activity, with the use of uridine 3'-(alpha-naphthylphosphate) or RNA as substrates, appears to be a valid diagnostic tool for pancreatic fibrosis in children.

  • References16
  • Citations18
  • References16
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Mentioned in this Paper

Enzymes, antithrombotic
Tissue Specificity
Benign Tumor of Pancreas
Cystic Fibrosis
Ribonuclease Activity
Alkaline Ribonuclease

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