Composition and Transport Function of Membranes of Chromaffin Granules: Established Facts and Unresolved Topics

Two dimensional electrophoresis has been established' as an essential tool for characterizing the membrane proteins ofchromath granules. Identified components with a known function include dopamine P-hydroxylase, cytochrome bSs,. subunits of the H+-ATF'ase (see below), actin, and a-actinin. Some functional proteins which have not yet been identified on 2D gels are the transporters for catecholamines, nucleotides, and calcium, and the carboxypeptidase H (enkephalin convFrtase)? Knowledge of the topology of the membranes is limited. Two facts seem established: (1) the carbohydrate chains of the membrane glycoproteins face the interior of the granule'"; and (2) a major part of the cytochrome bS1 molecule is present on the outer face of chromalk granule^.^ Evidence has been presented that most of the other proteins (including the ATPase and the phosphatidylinositol b a s e ) are also exposed on the outside of these organelles.' It is not clear, however, to what extent the various molecules are present in this position. In fact, Zaremba and HougeAngeletti' claim that the majority of proteins predominantly face the granule interior and have only some portion of their polypeptide chain facing the cytosol. Thus we

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