On the nature of the products formed by the action of crystalline ribonuclease (Kunitz's ribonuclease) on yeast ribonucleic acid.
Explore the source record for details and available documents.
SEARCH · Search PubMed
Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.
Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Using either DEAE-cellulose chromatography or pH 4--6 isoelectric focusing, we have separated mouse skeletal muscle neutral RNAase II-inhibitor complex into two fractions (designated alph and beta). para-Hydroxymercuriphenyl-sulfonate-induced dissociation/inactivation of the inhibitor yields free RNAase II enzyme fractions with differing pH profiles, CM-cellulose chromatographic behavior and reactivity with the RNAase II inhibitor of human placenta. However, the free RNAase fractions react equally with purified inhibitor from skeletal muscle and are not separable by pH 8--9.5 isoelectric focusing. These data suggest that mouse skeletal muscle has two heterogeneous forms of RNAase II. Additionally, heterologous RNAase II inhibitors may be used as investigational tools when probing neutral RNAase II heterogeneity.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
Explore the source record for details and available documents.