NDLI: Isolation of a clone of Chinese hamster ovary cells deficient in plant lectin-binding sites.

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Isolation of a clone of Chinese hamster ovary cells deficient in plant lectin-binding sites.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Gottlieb, C. Kornfeld, S. Skinner, A. M.
Abstract	Ricin, a galactose-binding lectin with potent cytotoxic activity, was used to select a clone of Chinese hamster ovary cells with altered plant lectin-binding properties. The clone (15B) is 80-fold less sensitive to the toxic action of ricin than the parent line. In the absence of ricin, it grows both in monolayer and suspension culture with a normal generation time. Plating efficiency, however, is significantly reduced. Relative to the parent cells, its binding of the Ricinus communis lectins, Phaseolus vulgaris erythroagglutinating phytohemagglutinin, Abrus precatorius phytohemagglutinin, and soybean phytohemagglutinin is less than 7%, while binding of lentil phytohemagglutinin, wheat-germ agglutinin, and mushroom phytohemagglutinin is 17%, 40%, and 109%, respectively. In contrast, its concanavalin A binding is increased by 70%. Consistent with these alterations, crude membrane preparations of the 15B cells were found to contain the same sugars as the parent-cell membranes but in different proportions. The 15B membranes have 28% less sialic acid, 38% less N-acetylglucosamine, 49% less galactose, the same amount of N-acetylgalactosamine, and 53% more mannose than the membranes of the parent cells.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	71
Language	English
Publisher	National Academy of Sciences
Publisher Date	1974-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Binding Sites, Antibody Clone Cells Immunology Lectins Animals Binding Sites Cell Membrane Cricetinae Iodine Radioisotopes Ovary Metabolism Ricin Pharmacology Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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