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    Negative influence of O-linked oligosaccharides of high molecular weight equine chorionic gonadotropin on its luteinizing hormone and follicle-stimulating hormone receptor-binding activities

    Date
    1996-06
    Author
    Butnev, Viktor Y.
    Gotschall, R. Russell
    Baker, Vanda L.
    Moore, William T.
    Bousfield, George R.
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    Citation
    Endocrinology. 1996 Jun; 137(6): 2530-42.
    Abstract
    Three equine CG (eCG) forms with identical amino acid sequences but different mol wt and monosaccharide compositions were isolated from a crude eCG preparation and designated eCG-L (low mol wt), eCG-M (medium mol wt), and eCG-H (high mol wt). No differences in primary structure between each form and the known sequence of eCG were observed. SDS-PAGE of these preparations under reducing conditions revealed that the mol wt differences between them were due only to the different sizes of their beta-subunits. Carbohydrate compositions suggested an increase in O-glycosylation in the higher mol wt forms. N-Linked glycopeptide fragments obtained from eCG beta-subunits by endoproteinase Lys-C digestion had identical electrophoretic mobilities. Thus, the different molecular sizes of the beta-subunits were associated only with disparities in O-glycosylation of their C-terminal extension. When tested in a LH and several FSH radioligand assay systems, eCG-H proved to have significantly lower receptor-binding activities than eCG-L and eCG-M. Endo-beta-galactosidase digestion increased the FSH receptor-binding activity of all eCG forms; however, partially deglycosylated eCG-H remained the least active form. Thus, the O-linked oligosaccharides of eCG-H exert a negative influence on its receptor-binding activity.
    Description
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    URI
    http://dx.doi.org/10.1210/en.137.6.2530
    http://hdl.handle.net/10057/4142
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