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By D. Rao Sanadi

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14C radioactivity; —, absorbance at 280 nm; . . , refractory index. (C) Automated solid-phase Edman degradation of the 21-residue fragment N-l resulted in the release of the bound carbodiimide label during step 8 (Hoppe and Sebald, 1980). (uiuu/sjunoo) e p i a i ) ! p o q j e o | A x a M O p A o i a [ 3 M] . e Q PROTEOLIPID S U B U N I T O F ATP S Y N T H A S E C O M P L E X 29 and the carboxyl groups of the glutamyl or aspartyl side chain is still u n k n o w n . In all studies on the identification of the carbodiimide-reactive 14 residue only tracer a m o u n t s of the C - l a b e l e d proteolipid w e r e u s e d , since the carbodiimide-modified and the free species of the proteolipid had not b e e n s e p a r a t e d .

H O P P E for the biogenesis, s t r u c t u r e , or function of this ATP s y n t h a s e subunit. + W h e n w e accept the idea that this protein translocates H across the m e m b r a n e , only the three invariant polar residues and possibly the peptide bonds in the polypeptide b a c k b o n e could b e catalytically involved + in the transport of the H . Especially, the only c o n s e r v e d acidic residue 65 ( G l u / A s p ) would b e a good c a n d i d a t e , since it is located in the middle of a hydrophobic segment (see also Section V).

As a m a t t e r of fact an oligomeric, probably h e x a m e r i c , structure of the proteolipid is indicated b y the a m o u n t of proteolipid present in the ATPase c o m p l e x (see Section VIII). T h e sensitivity of the m e m b r a n e - b o u n d A T P a s e c o m p l e x t o w a r d dicyclohexylcarbodiimide varies in different o r g a n i s m s . , 1971; L i n n e t and B e e c h e y , 1979). In o t h e r m e m b r a n e s , u n d e r c o m p a r a b l e conditions a 10- t o 50-fold molar e x c e s s of the carbodiimide has to be applied in o r d e r to a c h i e v e maximal inhibition.

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