Abstract
Trypsin-like and chymotrypsin-like esteroprotease isozymes of the mouse submandibular gland were separated by isoelectric focusing. In normal female mice the following pI-isozyme activities were found: pI−4.6, −5.6 (shoulder), −5.8, −7.1, and −9.9, hydrolytic activities for benzoylarginine ethylester (BAEE) (trypsin-like enzymes), and pI-4.7 and -10.3 hydrolytic activities for acetyltyrosine ethylester (ATEE) (chymotrypsin-like enzymes). In mice with testicular feminization (Tfm mice), only pI-4.6 hydrolytic activity for BAEE was found; no ATEE hydrolytic activity was detected. In normal female mice, both 5α-dihydrotestosterone (5α-DHT) and tri-iodo-L-thyronine (T3) significantly increased all these isozymes except the pI-4.6 hydrolytic activity for BAEE. In Tfm mice, T3 also increased all these isozymes except the pI-4.6 hydrolytic activity for BAEE, but 5α-DHT had no effect on any enzymes. These results suggest that the pI-4.6 hydrolytic activity for BAEE is non-inducible by the two hormones. Androgen does not seem to be involved in the inductions of these esteroproteases by T3.

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