title: Purification and properties of a ribonuclease from the excretory gland cells of Stephanurus dentatus.
abstract: Ribonuclease (RNase) was isolated and purified from the excretory gland cells of Stephanurus dentatus by (NH4)2SO4 fractionation, column chromatography on phosphocellulose and affinity chromatography using 5' -UTP-agarose. The purified enzyme hydrolyzed yeast RNA, cyclic nucleotides, and polynucleotides. Hydrolysis products of RNA and synthetic substrates were analyzed by column chromatography and/or thin-layer chromatography and the results indicated that S. dentatus RNase should be classified as an endoribonuclease (EC 3.1.27.1). Experimentally infected pigs produced antibodies against the RNase as shown by immunodiffusion and immunoelectrophoresis. The RNase was also secreted by adult worm into an in vitro maintenance medium. The RNase may function in the worm to degrade TNA as a source of nucleotides for metabolic purposes.
mesh_terms: D000818:Animals; D000917:Antibody Formation; D005088:Exocrine Glands / Q000201:enzymology; D005260:Female; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000378:metabolism; D007700:Kinetics; D008297:Male; D008970:Molecular Weight; D009348:Nematoda / Q000201:enzymology*; D012260:Ribonucleases / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism; D012265:Ribonucleotides / Q000378:metabolism; D017206:Strongylida Infections / Q000469:parasitology; D013379:Substrate Specificity; D013552:Swine
chemical_list: D007527:Isoenzymes; D012265:Ribonucleotides; D012260:Ribonucleases