Purification of envelope glycoproteins of human T cell lymphotropic virus type I (HTLV-I) by affinity chromatography.
J Virol Methods
; 18(4): 243-55, 1987 Dec.
Article
em En
| MEDLINE
| ID: mdl-2832431
ABSTRACT
The external envelope glycoprotein (gp46) and transmembrane glycoprotein (gp21) of human T-cell lymphotropic virus type I (HTLV-I) were isolated from lysates of HTLV-I-infected HUT-102 cells by affinity chromatography. Fifty ml aliquots of packed HUT-102 cells were extracted with 1% Triton X-100, and lysates were treated sequentially with an affinity column containing IgG from an HTLV-I+ human subject followed by chromatography of the bound fraction over a lentil lectin column. The identity of the purified envelope proteins was confirmed with a human monoclonal antibody (0.5 alpha) to gp46 and with rabbit antisera raised to a synthetic peptide from the C-terminus of gp21. Affinity-purified envelope glycoproteins were bound to microtiter wells and used in radioimmunoassay to detect murine and human anti-envelope antibodies to gp46 and gp21 molecules.
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Base de dados:
MEDLINE
Assunto principal:
Produtos do Gene env
/
Proteínas Oncogênicas de Retroviridae
/
Proteínas dos Retroviridae
/
Proteínas do Envelope Viral
/
Deltaretrovirus
Limite:
Humans
Idioma:
En
Ano de publicação:
1987
Tipo de documento:
Article