Significant Amount of Multicatalytic Proteinase Identified on Membrane from Human Erythrocyte
Multicatalytic proteinase (MCP) was solubilized from human erythrocyte membrane with 0.1% Triton X–100 and purified to homogeneity using a combination of DEAE-cellulose, hydroxylapatite, and Ultrogel AcA34 chromatographies. This membranous MCP had similar properties to MCP purified in parallel from...
Saved in:
Published in | Journal of biochemistry (Tokyo) Vol. 107; no. 3; pp. 440 - 444 |
---|---|
Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Oxford
Oxford University Press
01.03.1990
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Multicatalytic proteinase (MCP) was solubilized from human erythrocyte membrane with 0.1% Triton X–100 and purified to homogeneity using a combination of DEAE-cellulose, hydroxylapatite, and Ultrogel AcA34 chromatographies. This membranous MCP had similar properties to MCP purified in parallel from the cytosol. Both MCPs had a molecular mass of 570 kDa, were composed of apparently nine subunits of 22–36 kDa and had trypsin-and chymotrypsin-like activities. These activities were latent and required heating for the induction. However, slight differences were observed in the effects of reagents (DFP, monoiodoacetic acid, Mg2+, and Ca2+) between membranous and cytosolic MCP. The amount of MCP identified on membranes was estimated to be three-quarters or one-half of that found in the cytosol based on its trypsin- or chymotrypsin-like activity, respectively. |
---|---|
Bibliography: | 1This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan. ark:/67375/HXZ-130S48LC-7 2To whom correspondence and reprint requests should be addressed. istex:4B4D75E093358A00CF37694A4D47D054AB5DF7DE ArticleID:107.3.440 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-924X 1756-2651 |
DOI: | 10.1093/oxfordjournals.jbchem.a123064 |