Conserved N-terminal sequences in homologous subunits of the multicatalytic proteinase complex (proteasome)
作者:
ShivanandappaT.,
MargolisJoyce W.,
WagnerB. J.,
期刊:
Current Eye Research
(Taylor Available online 1991)
卷期:
Volume 10,
issue 9
页码: 871-876
ISSN:0271-3683
年代: 1991
DOI:10.3109/02713689109013883
出版商: Taylor&Francis
数据来源: Taylor
摘要:
The bovine lens multicatalytic proteinase complex (MFC) (MW 700 kDa) comprises at least twelve subunits in the molecular mass range 22–35 JcDa. Three of the subunits, LI (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. LI 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.
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