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Abstract：
Inhibitors of neutral ribonuclease have been purified to homogeneity from beef, pig, sheep, mouse, and rat liver by affinity chromatography on Sepharose-RNase A with overall yields ranging from 60-80%. Each of the purified inhibitors presents a single band by SDS-gel electrophoresis; molecular weight estimates by SDS-gel electrophoresis and by gel filtration are ca. 50 000. Each of the inhibitors forms a complex with beef pancreatic RNase A with a molecular weight of ca. 64 000, suggestive of 1:1 binding on a molar basis. The inhibitors from liver are very similar in properties and amino acid composition to the previously isolated inhibitor from human placenta (Blackburn et al. (1977) J. Biol. Chem. 252, 5904) and beef brain (Burton et al. (1980) Int. J. Peptide Protein Res. 16, 359). Pig liver offers an alternative to human placenta as a source for an RNase inhibitor of this type (yield, ca. 8 mg/kg of tissue). Immunological similarities were examined using antiserum directed against human placental RNase inhibitor. Cross reactivity of the liver RNase inhibitors with the antiserum raised against placental RNase inhibitor ranged from 15% for mouse RNase inhibitor to as low as 2% for pig and sheep RNase inhibitor.
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