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Title: Conserved N-terminal sequences in homologous subunits of the multicatalytic proteinase complex (proteasome). Author: Shivanandappa T, Margolis JW, Wagner BJ. Journal: Curr Eye Res; 1991 Sep; 10(9):871-6. PubMed ID: 1790717. Abstract: The bovine lens multicatalytic proteinase complex (MPC) (MW 700 kDa) comprises at least twelve subunits in the molecular mass range 22-35 kDa. Three of the subunits, L1 (27 kDa), L2 (24 kDa) and L3 (29 kDa), were purified by reverse phase HPLC. Their amino acid composition and N-terminal sequences indicate that they are not identical. L1 and L2 subunits show very high (greater than 90%) sequence homology with specific subunits of rat liver and human reticulocyte MPC and these are considered to be homologous components of the MPC which are highly conserved in evolution.[Abstract] [Full Text] [Related] [New Search]