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pubmed-article:8812855pubmed:abstractTextAffinity chromatography on immobilized ribonuclease (RNase) inhibitor was developed for purification of mammalian RNase. Human placental RNase inhibitor was conjugated to CNBr-activated Sepharose in the presence of dithiothreitol. About 80% of the immobilized RNase inhibitor was capable of binding bovine pancreatic RNase A. The bound RNase A was eluted with 3 M NaCl at pH 5.0. Two 25-kDa and 18-kDa RNases, which were obtained from human liver using a cellulose phosphate column, were bound to the immobilized RNase inhibitor and recovered in a pure and active form after treatment of the resin with p-hydroxymercuribenzoate. These enzymes were considered to be nonsecretory-type RNases with different sugar contents.lld:pubmed
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pubmed-article:8812855pubmed:articleTitlePurification of mammalian ribonuclease using immobilized human ribonuclease inhibitor.lld:pubmed
pubmed-article:8812855pubmed:affiliationDepartment of Legal Medicine, Fukui Medical School, Japan.lld:pubmed
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