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KMID : 0578319920020010043
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Molecules and Cells
1992 Volume.2 No. 1 p.43 ~ p.46
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A High Molecular Weight, Periplasmic Acid Protease (PAP) in Escherichi coli
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Park, Kyung Chan
Yoo, Jung Kwon/Kim, Seung Ho/Hahm, Kyung-Soo/Ha, Doo Bong/Chung, Chin Ha
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Abstract
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A protease with an acidic pH optimum was purified to near homogeneity from periplasm of Escherichia coli using [´H]globin as a substrate. This enzyme, referred to as periplasmic acid protease (PAP), has a size of 1.5 MDa under nondenaturing conditions. Polyacrylamide gel electrophoresis in the presence of SDS reveals that PAP consists of at least three subunits of 48, 39, and 35 kDa, indicating that it is a heteromultimeric enzyme. Since diisopropyl fluorophosphate inhibits the globin-degrading activity, it appears to be a serine protease. It is maximally active between pH 4.0 and pH 4.5, but has little activity above neutral pH. The physiological role of PAP is presently unknown.
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KEYWORD
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