Partial characterization of Fusobacterium necrophorum protease.
Partial characterization of Fusobacterium necrophorum protease was investigated. The protease was partially purified by gel filtration with Toyopearl HW 55. The final preparation was inactivated completely by heating at 60 degrees C for 30 min and inhibited by ascorbic acid, sodium thioglycollate and p-hydromercuribenzoate. Antibody response to the protease was demonstrated in mice receiving 10(4) CFU of F. necrophorum.
Nakagaki
M
M
Department of Veterinary Microbiology, Faculty of Agriculture, Yamaguchi University, Japan.
Fukuchi
M
M
Kanoe
M
M
D000907:Antibodies, Bacterial / Q000096:biosynthesis; D002850:Chromatography, Gel; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000737:chemistry / Q000276:immunology / Q000302:isolation & purification / Q000378:metabolism*; D005675:Fusobacterium necrophorum / Q000201:enzymology* / Q000276:immunology; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D011480:Protease Inhibitors / Q000494:pharmacology
D000907:Antibodies, Bacterial; D011480:Protease Inhibitors; D010450:Endopeptidases