Summary: Three proteinase isoenzymes from one benign strain of and five proteinase isoenzymes from each of two virulent strains of were purified by horizontal slab polyacrylamide gel electrophoresis. The purified isoenzymes hydrolysed casein, collagen I, collagen III, elastin, α-elastin, fibrinogen, gelatin, haemoglobin and α-keratin. The pH optima of all the isoenzymes lay between 7.25 and 9.5, the range of 8.75-9.25 being common to all. The isoenzymes were inhibited by phenylmethylsulphonyl fluoride, diphenylcarbamyl chloride, L-(l-tosylamide-2-phenyl)ethyl chloromethyl ketone, EGTA and EDTA, indicating that they were chymotrypsin-like serine proteinases that require a metal ion for stability or activity. EDTA inhibition was not reversed by addition of Ca or Mg. Some isoenzymes were activated by Mg, Ca, Cr and Se and all were inhibited by Fe, Co, Cu, Zn, Cd and Hg. Isoenzymes from benign strains had a lower temperature stability, losing all activity at 55°C, whereas those from virulent strains lost all activity at 60°C.


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