Immunofluorescent localization of 100K coated vesicle proteins.

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Immunofluorescent localization of 100K coated vesicle proteins

A family of coated vesicle proteins, with molecular weights of approximately 100,000 and designated 100K, has been implicated in both coat assembly and the attachment of clathrin to the vesicle membrane. These proteins were purified from extracts of bovine brain coated vesicles by gel filtration, hydroxylapatite chromatography, and preparative SDS PAGE. Peptide mapping by limited proteolysis in...

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Antibodies were raised in chickens against heterogeneous nuclear RNA (hnRNA)-binding proteins from 30S ribonucleoprotein (RNP) complexes of mouse Taper hepatoma ascites cell nuclei. The antibody preparations were characterized for immunological specificity and purity by double-diffusion gels, binding to specific bands in SDS polyacrylamide gels, and crossed immunoelectrophoresis. Antibodies rai...

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Immunocytochemical localization of coated vesicle protein in rodent nervous system

Immunocytochemistry has been used to study the distribution of the major 180,000-mol wt protein of coated vesicles in rodent cerebellum. An antibody to the coat protein was prepared in rabbits and characterized by immunodiffusion and immunofixation of polyacrylamide gels. At the light microscope level the protein was primarily localized in punctate profiles surrounding Purkinje cells and within...

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Identification of the coated vesicle proteins that bind calmodulin.

S 93,000 and 52,P0 were labeled. Specificity was demonstrated by the dependence of _L labeling on Ca , and by its reduction in the presence of unlabeled calmodulin or ,, Stelazine. Urea-soluble components of coated vesicles and material isolated by Sepharose CL4B chromatography formed a 52,000 MW labeled complex. Subtracting an apparent molecular weight of calmodulin of 20,000 from the weights ...

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Clathrin-coated vesicle formation: a paradigm for coated-vesicle formation.

Clathrin-coated pits are the major ports of entry into the cell and are responsible for the internalization of a variety of biologically important macromolecules. These transport intermediates form as a result of the co-ordinated assembly of a number of cytosolic proteins on to the membrane which results in specific cargo recruitment. We have used a variety of approaches including permeabilized...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 1986

ISSN: 0021-9525,1540-8140

DOI: 10.1083/jcb.102.1.48