Purification and properties of human acid-thermostable ribonucleases, and diagnosis of childhood pancreatic fibrosis.
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.
D002648:Child; D003300:Copper / Q000494:pharmacology; D003550:Cystic Fibrosis / Q000175:diagnosis* / Q000201:enzymology; D004386:Duodenum / Q000201:enzymology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009928:Organ Specificity; D010179:Pancreas / Q000201:enzymology; D012260:Ribonucleases / Q000097:blood / Q000302:isolation & purification / Q000378:metabolism*; D013154:Spleen / Q000201:enzymology; D015032:Zinc / Q000494:pharmacology
D003300:Copper; D012260:Ribonucleases; D015032:Zinc