THE EFFECTS OF N-GLYCOSYLATION ON THE LECTIN ACTIVITY OF RECOMBINANT RICIN B CHAIN
UNSPECIFIED (1991) THE EFFECTS OF N-GLYCOSYLATION ON THE LECTIN ACTIVITY OF RECOMBINANT RICIN B CHAIN. CARBOHYDRATE RESEARCH, 213 . pp. 19-25. ISSN 0008-6215Full text not available from this repository.
Soluble, biologically-active recombinant ricin B chain has been produced by expressing B chain-encoding DNA in heterologous eukaryotic or prokaryotic hosts. N-Glycosylated recombinant ricin B chain expressed in Xenopus oocytes bound to both immobilized asialofetuin and immobilized lactose. Nonglycosylated ricin B chain expressed in either E. coli or in tunicamycin-treated oocytes did not bind to immobilized lactose. However, it did bind to asialofetuin, and increasing concentrations of free lactose did not reduce this asialofetuin binding dramatically, in contrast to the effect of free lactose on the binding of either glycosylated recombinant B chain or native ricin B chain.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||CARBOHYDRATE RESEARCH|
|Publisher:||ELSEVIER SCIENCE BV|
|Date:||25 June 1991|
|Number of Pages:||7|
|Page Range:||pp. 19-25|
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