Purification of deformin, an extracellular protein synthesized by Bartonella bacilliformis which causes deformation of erythrocyte membranes.
Biochim Biophys Acta
; 1234(2): 173-83, 1995 Mar 22.
Article
en En
| MEDLINE
| ID: mdl-7696292
ABSTRACT
A factor capable of deforming erythrocyte membranes, found in the culture supernatants of Bartonella bacilliformis, was purified 1840-fold using hydrophobic, ion exchange and gel exclusion chromatography. The final fractions contained a single detectable polypeptide species, referred to as deformin, having a molecular weight of 67000 by SDS-PAGE and a native molecular weight of 130,000 by gel exclusion chromatography or velocity sedimentation in a glycerol gradient. Erythrocytes treated with deformin acquire trenches, indentations, and invaginations which could be reversed by vanadate, dilauroylphosphatidylcholine (DLPC), or by raising the internal Ca2+ concentrations with the inophore A23187. Internal vacuoles also form. Erythrocytes treated with trypsin or neuraminidase are much more sensitive to deformin than untreated erythrocytes; erythrocytes treated with phospholipase D are less sensitive to deformin. This protein may play a role in causing the severe anemia which can result as a consequence of infection by B. bacilliformis.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Bacterianas
/
Deformación Eritrocítica
/
Membrana Eritrocítica
Tipo de estudio:
Etiology_studies
Límite:
Humans
Idioma:
En
Revista:
Biochim Biophys Acta
Año:
1995
Tipo del documento:
Article