Summary: Membrane and cytoplasmic fractions of inhibited the multiplication of this mycoplasma. Arginine deiminase (EC, isolated from both fractions, reproduced the inhibition. The purified cytoplasmic deiminase had a subunit of 49000, a specific activity of 53 units (mg protein) and an / ratio of 1·76. The membrane-associated enzyme had an identical but lower values for specific activity [39 units (mg protein)] and the / ratio (1·46). In experiments , recent clinical isolates of produced less arginine deiminase, but grew faster than the laboratory reference strain PG 21. In addition, other growth inhibitory components associated with membrane preparations were detected in recent clinical isolates but were absent from strain PG 21.


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