Restoration of lectin activity to a non-glycosylated ricin B chain mutant by the introduction of a novel N-glycosylation site
UNSPECIFIED. (1997) Restoration of lectin activity to a non-glycosylated ricin B chain mutant by the introduction of a novel N-glycosylation site. FEBS LETTERS, 407 (3). pp. 271-274. ISSN 0014-5793Full text not available from this repository.
Ricin B chain (RTB) is an N-glycosylated, galactose-specific lectin, Removal of the two native N-glycosylation sites at Asn(95) and Asn(135) by site-directed mutagenesis generated a recombinant protein devoid of lectin activity, Two novel N-glycosylation sites were introduced into RTB at Asn(42) and Asn(123), either singly or in combination, Microinjection of pre-RTB transcripts into Xenopus oocytes showed that these novel sites became glycosylated in vivo, The single oligosaccharide site chain at Asn(42) restored lectin activity to RTB, whereas glycosylation at Asn(123) or simultaneous glycosylation at Asn(42) and Asn(123) failed to do so. (C) 1997 Federation of European Biochemical Societies.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||FEBS LETTERS|
|Publisher:||ELSEVIER SCIENCE BV|
|Date:||5 May 1997|
|Number of Pages:||4|
|Page Range:||pp. 271-274|
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