锌羧肽酶A和脱辅基羧肽酶A的蛋白酶敏感性

Protease susceptibility of zinc- and apo-carboxypeptidase A.

作者信息

Bicknell R, Schaeffer A, Auld D S, Riordan J F, Monnanni R, Bertini I

出版信息

Biochem Biophys Res Commun. 1985 Dec 17;133(2):787-93. doi: 10.1016/0006-291x(85)90973-8.

Abstract

Proteases in preparations of carboxypeptidase A progressively inactivate solutions of the apoenzyme but not the metal-containing enzyme. Free amino acids generated by proteolysis interfere with spectral studies after reconstituting the apoenzyme with cobalt. Purification by affinity chromatography eliminates this effect. Affinity-purified apoenzyme is susceptible to digestion with chymotrypsin but the metalloenzyme is not.

摘要

羧肽酶A制剂中的蛋白酶会逐渐使脱辅基酶溶液失活，但不会使含金属的酶失活。蛋白水解产生的游离氨基酸在将脱辅基酶与钴重构后会干扰光谱研究。通过亲和层析纯化可消除这种影响。亲和纯化的脱辅基酶易被胰凝乳蛋白酶消化，但金属酶则不易被消化。