Significant amount of multicatalytic proteinase identified on membrane from human erythrocyte.
J Biochem
; 107(3): 440-4, 1990 Mar.
Article
em En
| MEDLINE
| ID: mdl-2187858
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cisteína Endopeptidases
/
Membrana Eritrocítica
/
Complexos Multienzimáticos
Limite:
Humans
Idioma:
En
Revista:
J Biochem
Ano de publicação:
1990
Tipo de documento:
Article