Molecular cloning and characterization of an extracellular protease gene from Aeromonas hydrophila.
A structural gene which codes for an extracellular protease in Aeromonas hydrophilia SO2/2 and D13 was cloned in Escherichia coli C600-1 by using pBR322 as a vector. The gene codes for a temperature-stable protease with a molecular mass of approximately 38,000 daltons. The protein was secreted to the periplasm of E. coli C600-1 and purified by osmotic shock. Cloned protease (P3) was identical in molecular mass and properties to the one purified from A. hydrophila SO2/2 culture supernatant as an extracellular product.
Departmento de Patologia Animal (Sanidad Animal), Unidad de Microbiología, Facutad de Veterinaria, Universidad de León, Spain.
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Rivero
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Anguita
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Paniagua
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Naharro
D000333:Aeromonas / Q000201:enzymology / Q000235:genetics*; D002876:Chromosomes, Bacterial; D003001:Cloning, Molecular / Q000379:methods; D004269:DNA, Bacterial / Q000235:genetics / Q000302:isolation & purification; D004926:Escherichia coli / Q000235:genetics; D005798:Genes, Bacterial; D007700:Kinetics; D009693:Nucleic Acid Hybridization; D010447:Peptide Hydrolases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D010957:Plasmids; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D015183:Restriction Mapping
D004269:DNA, Bacterial; D011994:Recombinant Proteins; D010447:Peptide Hydrolases