Studies on esteroproteases in the mouse submaxillary gland:Purification and properties of the isozymes

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Recently we have reported that these was a marked strain difference in arginine-specific esteroprotease isozymes found in the submaxillary gland of inbred mice. The present study was designed to clarify the properties of the esteroprotease isozymes in the submaxillary gland of mice.<BR>Three esteroproteases (isozymes III, N and IX) and two esteroproteases (isozymes VI and VIII) were purified from the two strains, BALB/cA and DBA/2N male mice, respectively, by gel filtration and column isoelectric focusing. Each of the purified isozymes appeared as a single protein band with polyacrylamide gel electrophoresis.<BR>The isoelectric points of the five isozymes were 5.6, 5.9, 7.6, 8.8 and 9.8 in isozymes III, IV, VI, VIII and IX, respectively. The five isozymes had a common molecular weight of about 28, 000 and the activities to hydrolyze α-N-benzoyl-L-arginine ethyl ester were not reduced by treating them for 1 hour at 40°C.<BR>Although a marked difference was found in substrate specificity when tested with various synthetic substrates, amino acid compositions of the enzymes closely resembled each other among the five isozymes.
歯科基礎医学会の論文