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By Bernard L. Horecker, Earl R. Stadtman

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By ( N H ) S 0 fractionation of an extract of perfused m u s c l e , t w o inhibitors ( M W 15,000 and 30,000) w e r e s e p a r a t e d from the p r o t e i n a s e (18). K o p i t a r and L e b e z (77) isolated a trypsin-like e n z y m e from the granules of hog blood l e u k o c y t e s and found that the l e u k o c y t e cytosol contained an inhibitor ( M W 43,000) of the granule p r o t e i n a s e . S t e v e n et al. (146) p r e p a r e d a similar e n z y m e from the granules of l e u k o c y t e s obtained from 4 2 4 34 JAMES F.

B e y n o n a n d K a y (11) studied a trypsin-like serine proteinase p r e s e n t in rat intestinal s m o o t h m u s c l e . This e n z y m e is of particular interest b e c a u s e it has a m a r k e d ability to inactivate native e n z y m e s in vitro. By ( N H ) S 0 fractionation of an extract of perfused m u s c l e , t w o inhibitors ( M W 15,000 and 30,000) w e r e s e p a r a t e d from the p r o t e i n a s e (18). K o p i t a r and L e b e z (77) isolated a trypsin-like e n z y m e from the granules of hog blood l e u k o c y t e s and found that the l e u k o c y t e cytosol contained an inhibitor ( M W 43,000) of the granule p r o t e i n a s e .

5 in an a t t e m p t to p r e p a r e I without I . Purification by passage through a S e p h a d e x G-75 column and then a hydroxylapatite column p r o d u c e d t w o well-separated I p e a k s . T h e s e t w o fractions w e r e tested against 11 different proteinases with the results s h o w n in Table V. B o t h inhibited hog kidney and rat liver cathepsin H but had little or no activity against bovine spleen or rat liver cathepsin B. It w a s s o m e w h a t u n e x p e c t e d to find s o m e differences b e t w e e n the t w o fractions and to o b s e r v e that they inhibited certain plant cysteine pro­ teinases but not o t h e r s .

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