Purification and properties of human acid-thermostable ribonucleases, and diagnosis of childhood pancreatic fibrosis.
Clin Chim Acta
; 67(3): 231-43, 1976 Mar 15.
Article
em En
| MEDLINE
| ID: mdl-4243
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ribonucleases
/
Fibrose Cística
Tipo de estudo:
Diagnostic_studies
Limite:
Child
/
Humans
Idioma:
En
Revista:
Clin Chim Acta
Ano de publicação:
1976
Tipo de documento:
Article