Franklin S G, Metrione R M
Biochem J. 1972 Mar;127(1):207-13. doi: 10.1042/bj1270207.
Preparations of ox spleen cathepsin B1 have been found to give multiple peaks of activity upon chromatography on DEAE-cellulose in NaCl gradients or by equilibrium chromatography in 0.05m-NaCl. CM-cellulose gradient chromatography also shows several cathepsin B1 peaks. This evidence indicates that ox spleen cathepsin B1 can exist in at least three to five forms. All forms have the same molecular weight, are thiol-activated and are inhibited by typical thiol inhibitors. The possible sources of this multiplicity of activity are discussed and a possible physiological role for cathepsin B2 is suggested.
已发现，牛脾组织蛋白酶B1制剂在NaCl梯度中于DEAE-纤维素上进行层析，或在0.05m-NaCl中进行平衡层析时，会出现多个活性峰。CM-纤维素梯度层析也显示出几个组织蛋白酶B1峰。这一证据表明，牛脾组织蛋白酶B1至少可以以三到五种形式存在。所有形式都具有相同的分子量，是硫醇激活的，并受到典型硫醇抑制剂的抑制。文中讨论了这种活性多样性的可能来源，并提出了组织蛋白酶B2可能的生理作用。
