[Cytolytic activity of Legionella pneumophila].
The properties of cytolysin and metalloproteinase purified by different methods have been studied. The physico-chemical properties of these proteins, including their molecular weight, immunodiffusion patterns, the degree of inhibition by EDTA and diethyl pyrocarbonate, amino acid composition, cytolytic and proteolytic activity, have proved to be similar. We have come to the conclusion that cytolysin and metalloproteinase have similar composition and metalloproteinase activity determines the cytolytic and necrotic activity of the above-mentioned cytolysin.
Belyĭ
Iu F
IuF
Tartakovskiĭ
I S
IS
Gul'nik
S V
SV
Lavreneva
G I
GI
Stepanov
V M
VM
D000596:Amino Acids / Q000032:analysis; D003603:Cytotoxins / Q000302:isolation & purification*; D006868:Hydrolysis; D005779:Immunodiffusion; D007875:Legionella / Q000201:enzymology / Q000378:metabolism* / Q000472:pathogenicity; D008666:Metalloendopeptidases / Q000378:metabolism*; D008970:Molecular Weight
D000596:Amino Acids; D003603:Cytotoxins; D008666:Metalloendopeptidases
Priroda tsitoliticheskoĭ aktivnosti Legionella pneumophila.