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Conserved N-terminal sequences in homologous subunits of the multicatalytic proteinase complex (proteasome)
T Shivanandappa1, J W Margolis, B J Wagner
1Department of Biochemistry and Molecular Biology, UMDNJ-New Jersey Medical School, Newark 07103-2714.
Current Eye Research
|September 1, 1991
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.