Huse K, Kopperschläger G, Hofmann E
Acta Biol Med Ger. 1982;41(11):991-1002.
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.
通过以D，L - 酪氨酸乙酯为配体进行亲和层析，将面包酵母中的蛋白酶B纯化至同质。该产物的分子参数与其他研究小组先前报道的相似。如果用CM - 纤维素层析和凝胶过滤代替亲和层析，则会分离出一种不同形式的蛋白酶B。在这种情况下，发现有一种与该酶紧密结合的肽段。这可以被鉴定为蛋白酶A诱导的蛋白酶B结合抑制剂经有限蛋白水解产生的抑制剂片段。
