PMID:7037737
| Citation |
Swamy, KH and Goldberg, AL (1982) Subcellular distribution of various proteases in Escherichia coli. J. Bacteriol. 149:1027-33 |
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| Abstract |
It has been reported recently that Escherichia coli cells contain eight 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 restriction to the cytoplasm. The six 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 one (Re) is distributed equally between the two cellular fractions. The others are present only in the cytoplasm. |
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| Keywords |
Adenosine Triphosphate/pharmacology; Caseins/metabolism; Cytoplasm/enzymology; Escherichia coli/enzymology; Escherichia coli/ultrastructure; Globins/metabolism; Insulin/metabolism; Membranes/enzymology; Peptide Hydrolases/analysis; Peptide Hydrolases/metabolism; Ribosomes/enzymology; Subcellular Fractions/enzymology |
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