牛脑氨肽酶的研究。

Brecher A S, Sobel R E

Biochem J. 1967 Nov;105(2):641-6. doi: 10.1042/bj1050641.

Mn(2+)-inhibited and Mn(2+)-activated aminopeptidases have been observed in ox brain and separated from one another by DEAE-cellulose column chromatography. 2. The Mn(2+)-inhibited enzyme has been purified 36-fold; it exhibits a specificity for tripeptide substrates, whereas the Mn(2+)-activated aminopeptidase cleaves dipeptides as well as tripeptides. 3. Ammonium sulphate treatment generates a Mn(2+)-stimulated aminopeptidase that is stable to dialysis against EDTA and water, in contrast with an endogenous Mn(2+)-activated preparation that is irreversibly denatured by such dialysis against EDTA and water.

在牛脑中观察到锰离子抑制型和锰离子激活型氨肽酶，并用二乙氨基乙基纤维素柱色谱法将它们彼此分离。2. 锰离子抑制型酶已被纯化36倍；它对三肽底物具有特异性，而锰离子激活型氨肽酶既能切割二肽也能切割三肽。3. 硫酸铵处理产生一种锰离子刺激型氨肽酶，该酶对用乙二胺四乙酸和水进行透析稳定，这与内源性锰离子激活型制剂不同，后者经用乙二胺四乙酸和水进行透析会不可逆地变性。

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核心技术专利：CN118964589B侵权必究

Brecher A S, Sobel R E

Biochem J. 1967 Nov;105(2):641-6. doi: 10.1042/bj1050641.

Mn(2+)-inhibited and Mn(2+)-activated aminopeptidases have been observed in ox brain and separated from one another by DEAE-cellulose column chromatography. 2. The Mn(2+)-inhibited enzyme has been purified 36-fold; it exhibits a specificity for tripeptide substrates, whereas the Mn(2+)-activated aminopeptidase cleaves dipeptides as well as tripeptides. 3. Ammonium sulphate treatment generates a Mn(2+)-stimulated aminopeptidase that is stable to dialysis against EDTA and water, in contrast with an endogenous Mn(2+)-activated preparation that is irreversibly denatured by such dialysis against EDTA and water.

在牛脑中观察到锰离子抑制型和锰离子激活型氨肽酶，并用二乙氨基乙基纤维素柱色谱法将它们彼此分离。2. 锰离子抑制型酶已被纯化36倍；它对三肽底物具有特异性，而锰离子激活型氨肽酶既能切割二肽也能切割三肽。3. 硫酸铵处理产生一种锰离子刺激型氨肽酶，该酶对用乙二胺四乙酸和水进行透析稳定，这与内源性锰离子激活型制剂不同，后者经用乙二胺四乙酸和水进行透析会不可逆地变性。