Subcellular distribution of various proteases in Escherichia coli.
- 1 January 1982
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 149 (3) , 1027-1033
- https://doi.org/10.1128/jb.149.3.1027-1033.1982
Abstract
E. coli cells contain 8 distinct soluble enzymes capable of degrading proteins to acid-soluble material. Two are metalloproteases that degrade [125I]insulin but not larger proteins: protease PI, which is identical to protease III, is restricted to the periplasm, and protease Ci is restricted to the cytoplasm. The 6 others (named Do, Re, Mi, Fa, So and La, which is the ATP-dependent protease) are serine proteases that degrade [14C]globin and [3H]casein, but not insulin. One of these (Mi) is localized to the periplasm, and 1 (Re) is distributed equally between the 2 cellular fractions. The others are present only in the cytoplasm.This publication has 48 references indexed in Scilit:
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