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Conserved N-terminal sequences in homologous sub-units of the multicatalytic proteinase complex (proteasome).

Shivanandappa, T. and Margolish, J. W. and Wagner, D. J. (1991) Conserved N-terminal sequences in homologous sub-units of the multicatalytic proteinase complex (proteasome). Current Eye Research, 10. pp. 871-876.

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Abstract

The bovine lens multicatalytic proteinase complex (MPC) (HW 100 kDa) comprises at least twelve subunits in the molecular mass range 22-35 kDa. Three of the subunits, Ll (27 kDa), L2 (24 kDa) and L3 (29 kDa) , were purified by reverse phase HPLC. Their amino acid composition and Nterminal sequences indicate that they are not identical. Ll and L2 subUnits show very high (>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.

Item Type: Article
Uncontrolled Keywords: multicatalytic proteinase complex bovine lens
Subjects: 500 Natural Sciences and Mathematics > 11 Animals
Divisions: Food Protectants and Infestation Control
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 03 Jan 2017 12:26
Last Modified: 03 Jan 2017 12:26
URI: http://ir.cftri.com/id/eprint/3593

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