Human ribonucleases. Quantitation of pancreatic-like enzymes in serum, urine, and organ preparations.
Antibodies against pure human pancreatic ribonuclease (RNase) were used to study ribonuclease levels in human tissues and body fluids. The antibodies completely inhibit the activity of purified RNase as well as ribonuclease activity in crude pancreatic extracts. RNase activity is inhibited by 70-80% in serum and urine, indicating that a significant proportion of the RNases in these preparations are structurally like the pancreatic enzyme. In contrast, inhibition of RNase activities from spleen (8%) and liver (30%) was inefficient suggesting that most of the RNases in these tissues are structurally unlike the pancreatic enzyme. A competitive binding radioimmunoassay (RIA), sensitive in the range of 1-100 ng of RNase, was developed to quantitate the pancreatic like enzymes. The RIA of crude tissue preparations and samples fractionated by gel filtration was compatible with inhibition results. Enzymes structurally like pancreatic RNase could be quantitated despite the presence of other RNase activities. Immunological quantitation of pancreatic like RNases was also found to be much more simple and precise than enzymatic assays comparing RNA and polycytidylate substrates. We suggest the immunological assays will be useful in the quantitation and definition of tissue of origin of RNases in serum of patients with pancreatic carcinoma.
D001667:Binding, Competitive; D002850:Chromatography, Gel; D003429:Cross Reactions; D004720:Endonucleases / Q000032:analysis*; D006801:Humans; D011863:Radioimmunoassay / Q000379:methods; D012259:Ribonuclease, Pancreatic; D012260:Ribonucleases / Q000032:analysis*; D014018:Tissue Distribution
D004720:Endonucleases; D012260:Ribonucleases; D012259:Ribonuclease, Pancreatic