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.res.in/id/eprint/3593

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