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A Membrane-Bound Protease in Microsomes of Spinach Callus

Institute of Biological Sciences, University of Tsukuba, Sakura-mura, Ibaraki 305, Japan

A di-isopropyl phosphorofluoridate-sensitive endopeptidase activity against some minor components of heat-denatured -casein was detected in the endoplasmic reticulum and Golgi body-rich fraction of spinach callus. The activity was not solubilized with 0.05% sodium deoxycholate, but with 0.5% sodium cholate. The activity was strongly inhibited by deoxycholate (0.2-0.5%), di-isopropyl phosphorofluoridate, p-chloro-mercuric benzoate, o-phenanthroline, NiCl₂, CuCl₂, and ZnSO₄, and moderately by phenylmethylsulfonyl fluoride, L-1-tosylamide-2-phenylethyl chloromethyl ketone, iodoacetic acid, ethylenediaminetetraacetate, and FeSO₄, and slightly by chymostatin. The inhibitory effect of o-phenanthroline was partially recovered with the addition of FeSO₄ and ZnSO₄.