Journal of Biological Chemistry · 1987 · 116 citations · 52 references
Life SciencesBiochemistryEgg ScienceLipid BiochemistryProtein BiochemistryLipid-protein InteractionsLipoprotein AnalysisProtein AnalysisProtein-lipid InteractionsApolipoprotein B-containing LipoproteinsLipoprotein BindingLipoprotein Receptor Binding AnalysisLipoprotein ReceptorsLow-density Lipoprotein Receptor FamilyPolyclonal AntibodiesReceptorsSodium Dodecyl Sulfate-polyacrylamide Gel Electrophoresis
The chicken oocyte receptor for low and very low density lipoproteins has been identified and characterized. Receptor activity present in octyl-beta-D-glucoside extracts of oocyte membranes was measured by a solid phase filtration assay, and the receptor was visualized by ligand blotting. The protein had an apparent Mr of 95,000 in sodium dodecyl sulfate-polyacrylamide gels under nonreducing conditions and exhibited high affinity for apolipoprotein B-containing lipoproteins, but not for high density lipoproteins or lipoproteins in which lysine residues had been reductively methylated. Binding of lipoproteins was sensitive to EDTA, suramin, and treatment with Pronase. In these aspects, the avian oocyte system was analogous to the mammalian low density lipoprotein receptor in somatic cells. Furthermore, a structural relationship between the mammalian and avian receptors was revealed by immunoblotting: polyclonal antibodies directed against the purified bovine low density lipoprotein receptor reacted selectively with the 95-kDa chicken receptor present in crude oocyte membrane extracts.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
Michael S. Brown, Joseph L. Goldstein · Proceedings of the National Academy of Sciences · 1974 · 598 citations · Full text