Slow moving protease (SMP), a non-pepsinogen type acid protease present in human gastric muscosa, was purified to apparent homogeneity by an improved purification procedure including chromatography on DEAE-cellulose, concanavalin A-Sepharose and Sephadex G-150. Upon DEAE-cellulose chromatography, SMP was separated into three fractions, designated SMP-I, SMP-II, and SMP-III. SMP-I was the major component and the other two appeared to be autodigestion products of SMP-I. Investigation on the specificity of action of SMP on the B chain of oxidized insulin revealed that SMP resembles cathepsin E and pepsin A in substrate specificity rather than cathepsin D and pepsin C.
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Matsuzaki et al. (1988) studied this question.
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