A high molecular weight, periplasmic acid protease(PAP) in Escherichia coli

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Title
A high molecular weight, periplasmic acid protease(PAP) in Escherichia coli
Author(s)
Kyung Chan Park; Jugn Kwon Yoo; Seung Ho Kim; Kyung Soo Hahm; Doo Bong Ha; Chin Ha Chung
Bibliographic Citation
Molecules and Cells, vol. 2, no. 1, pp. 43-46
Publication Year
1992
Abstract
A protease with an acidic pH optimum was purified to near homogeneity from periplasm of Escherichia coli using L3H]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.
ISSN
1016-8478
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
Division of Biomedical Research > Personalized Genomic Medicine Research Center > 1. Journal Articles
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