Clathrin heavy chain, light chain interactions.
作者： F.K. Winkler , K.K. Stanley
DOI: 10.1002/J.1460-2075.1983.TB01597.X
关键词:
摘要: Purified pig brain clathrin can be reversibly dissociated and separated into heavy chain trimers light chains in the presence of non-denaturing concentrations chaotrope thiocyanate. The isolated reassemble regular polygonal cage structures absence chains. fraction further resolved its two components L alpha beta which give different one-dimensional peptide maps. Radiolabelled bind with high affinity (KD < 10(-10) M) to trimers, cages a 110,000 mol. wt. tryptic fragment chain. Both compete each other from sources for same binding sites on c.d. spectroscopy shows that possess very similar structures. We conclude sources, despite some heterogeneity, have highly conserved, site but are not essential formation
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