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KMID : 0578319930030020153
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Molecules and Cells
1993 Volume.3 No. 2 p.153 ~ p.156
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Purification and Partial Characterization of a Latent Serine Protease in Escherichia coli
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Yoo, Jung kwon
Park, Kyung Chan/woo, Seung Kyoon/Woo, Kee Min/Ha, Doo Bong/Chung, Chin Ha
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Abstract
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A new serine protease has been purified from Escherichia coli by conventional chromatographic procedures using [´H]-casein as a substrate. It h-s an apparent size of about 34 kDa as determined by gel filtration on a Superose-12 column. The purified enzyme, however, consisted of two polypeptides with 16 and 12-kDa when analyzed by polyacrylamide gel electrophoresis in the presence of sodium dodesyl sulfate. These results suggest that the protease is a heterodimeric complex. The casein-degrading activity of the protease was completely inhibited by I mM diisopropyl fluorophosphate. It was also sensitive to inhibition by metal chelating agents including EDTA and o-phenanthrohne, suggesting that the enzyme belongs to a family of serine proteases. Interestingly, the enzyme activity could he enhanced 5- to 20-fold by incubation at 4 C for about 3 weeks. Therefore, this new protease was named as LSP (Latent Serine Protease). LSP was maximally active at pH between 5.5 and 9.5. The activation mechanism and physiological role of this protease are presently uni -own.
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