Analysis of 100 kDa polypeptides from coated vesicles of bovine brain: two-dimensional tryptic and chymotryptic maps.
Two-dimensional peptide map analysis was used to determine the structural homology among the '100 kDa'-group of polypeptides. There are at least six distinct polypeptides whose apparent molecular weights are 116, 113, 111, 108, 105 and 100 kDa. The molar ratio of the '100 kDa'-group of polypeptides to three clathrin monomers (equivalent to one triskelion) is 1.2:1. There are three families of polypeptides in the '100 kDa'-group as determined by two-dimensional peptide map analysis. They are 116 and 113 kDa polypeptides, 111, 108, and 105 kDa polypeptides and 100 kDa polypeptide. However, all six polypeptides apparently show a series of homologous peptides. It is suggested that the 100-116 kDa polypeptides may bind to triskelions at the area of homology that is found in the 100-116 kDa polypeptides.
D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002918:Chymotrypsin; D002966:Clathrin / Q000032:analysis; D003034:Coated Pits, Cell-Membrane / Q000032:analysis*; D003594:Cytoplasmic Granules / Q000032:analysis*; D011992:Endosomes / Q000032:analysis*; D007425:Intracellular Membranes / Q000032:analysis; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000032:analysis*; D010449:Peptide Mapping; D014357:Trypsin
D002966:Clathrin; D009419:Nerve Tissue Proteins; D002918:Chymotrypsin; D014357:Trypsin