By Bernard L. Horecker, Earl R. Stadtman
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Additional resources for Current topics in cellular regulation. Vol.17
Adapted from Knight and Barrett (75). the separation by gel filtration of a protein and a low-molecular-weight ligand. Nichol and W i n z o r (108) and Gilbert (49) have analyzed by frontal analysis the special situation in which the e n z y m e and its inhibitor have approximately equal size. In this and other cases w h e r e dissociation is partial, the elution v o l u m e of the protein p e a k consisting of the complex and its trailing but overlapping free c o m p o n e n t s is greater than that of the complex itself.
Bernik and K w a a n (9) described three immunologically distinct types of plasminogen a c t i v a t o r s . Fetal lung and kidney tissues cultured in serumfree m e d i u m secreted a proteinase resembling u r o k i n a s e , as well as an inhibitor of this e n z y m e . Loskutoff and Edgington (91) noted that a mem b r a n e fraction from vascular endothelial cells displayed plasminogen ac tivator activity, and that the cytosol from these cells inhibited this en z y m e . W h o l e h o m o g e n a t e s w e r e inactive, but acidification to p H 3 d e s t r o y e d the inhibitor and u n m a s k e d the proteinase activity.
5 - 3 . 0 . Figure 2 illustrates that m a x i m u m yields of both inhibitors w e r e obtained in this p H range. By heating at p H 8, an extract containing I with no I w a s p r e p a r e d . Table IV s h o w s the distribution of I and I in various rat and h u m a n tissues. Five additional rat tissues w e r e a n a l y z e d ; all contained I and I . 6 to 52, suggesting that the inhibitors w e r e t w o s e p a r a t e proteins rather than a single double-headed inhibitor of b o t h e n z y m e s .
Current topics in cellular regulation. Vol.17 by Bernard L. Horecker, Earl R. Stadtman