Open Access@KRIBBDivision of A.I. & Biomedical ResearchGenomic Medicine Research Center1. Journal Articles
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 A.I. & Biomedical Research > Genomic Medicine Research Center > 1. Journal Articles
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