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Title: A new procedure for the purification of proteinase B from baker's yeast and interaction of the purified enzyme with a specific inhibitor. Author: Huse K, Kopperschläger G, Hofmann E. Journal: Acta Biol Med Ger; 1982; 41(11):991-1002. PubMed ID: 6763433. Abstract: Proteinase B from baker's yeast was purified to homogeneity by applying affinity chromatography with D,L-tyrosine ethyl ester as ligand. The molecular parameters of the product are similar to those reported formerly by other groups. A different form of proteinase B is isolated if affinity chromatography is replaced by CM-cellulose chromatography and gel filtration. In this case a peptide tightly associated with the enzyme was found to occur. This could be identified as an inhibitor fragment produced by limited proteolysis of a proteinase B bound inhibitor induced by proteinase A.[Abstract] [Full Text] [Related] [New Search]