Heat-stable proteases from psychrotrophic pseudomonads: comparison of immunological properties.
A heat-stable extracellular protease from Pseudomonas fluorescens was purified by chromatography on a DEAE-cellulose column and gel filtration on a Sephadex G100 column. The homogeneous enzyme preparation was used to prepare antiserum in rabbits. The rabbit antiserum was used to study the antigenic relatedness of proteases from 19 psychrotrophic pseudomonads isolated from raw milk. The inhibition of the proteases by the antiserum and the gel precipitin reactions revealed similar antigenic determinants in proteases from different isolates. Rabbit antiserum to the purified protease gave precipitin bands with antigens (proteases) from 10 different isolates. However, the same antiserum did not inhibit the protease activity in cell extracts of isolates T10, T13, and T24. By determining serological cross-reactions, proteases from psychrotrophic pseudomonads were shown to be different from one another.
D000818:Animals; D002364:Caseins / Q000378:metabolism; D003080:Cold Temperature; D003429:Cross Reactions; D000939:Epitopes / Q000276:immunology; D006358:Hot Temperature; D008892:Milk / Q000382:microbiology; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000276:immunology* / Q000302:isolation & purification / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology* / Q000302:isolation & purification; D011551:Pseudomonas fluorescens / Q000201:enzymology*
D002364:Caseins; D000939:Epitopes; D010447:Peptide Hydrolases