A new procedure for the purification of proteinase B from baker's yeast and interaction of the purified enzyme with a specific inhibitor.
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.
D002846:Chromatography, Affinity; D010450:Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D011480:Protease Inhibitors / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000032:analysis*
D011480:Protease Inhibitors; D010450:Endopeptidases