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Thiol-Sepharose binding proteins

Membrane extracts from adult H. contortus were enriched 24-fold for cysteine protease activity by passage over a Thiol-Sepharose affinity column and the proteins obtained (abbreviated as TSBP) were clearly localized to the microvillar surface of the intestinal cells (Knox et al., 1995,1999). TSBP comprised a prominent 60 kDa protein and several minor bands between 35 and 45 kDa and 97 to 120 kDa (Fig. 13.2). Protease activity at 38, 52 and 70 kDa was attributable to cysteine proteases and at 70 and 88 kDa to serine/metalloproteases, as judged by inhibition analyses. Lectin-binding studies showed that most of the TSBPs were glycosylated. Expression library... [Pg.266]


See other pages where Thiol-Sepharose binding proteins is mentioned: [Pg.264]    [Pg.264]    [Pg.520]    [Pg.521]    [Pg.453]    [Pg.5]    [Pg.448]    [Pg.95]    [Pg.168]   


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Sepharose

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