Multiple proteinases from two Microsporum species.
Enzyme expression of 67 isolates of two Microsporum species, M. canis and M. cookei, were compared in both shake and stationary cultures using substrate copolymerized SDS-PAGE. Most M. canis isolates expressed more proteolytic bands in shake culture, while M. cookei isolates expressed more in stationary culture. M. canis isolates expressed up to six proteinases of different relative mobilities (122, 64, 62, 45, 31 and 25 kDa). M. cookei expressed up to seven proteinases in stationary culture (67, 66, 64, 62, 45, 42 and 39 kDa). Those of 67 and 66 kDa were not expressed in shake culture. The proteinases expressed by M. cookei were similar to those expressed by M. canis except for 122 and 25 kDa. With the exception of isolates from non-infected cats, 25 kDa was also commonly expressed by isolates from infected hosts in the shake culture treatment. The differences in enzyme expression obtained may reflect differences in the contrasting ecological roles of the two species.
Simpanya
M F
MF
Department of Microbiology and Genetics, Massey University, Palmerston North, New Zealand. MSimpanya@p5.fl.n.761.z5.fidonet.org
Baxter
M
M
D000818:Animals; D002415:Cats; D003881:Dermatomycoses / Q000382:microbiology*; D004285:Dogs; D018093:Gelatinases / Q000378:metabolism*; D006801:Humans; D008864:Microsporum / Q000201:enzymology* / Q000302:isolation & purification; D009172:Mycology / Q000379:methods; D013045:Species Specificity
D018093:Gelatinases