Fever and hypothermia in systemic inflammation: recent discoveries and revisions.
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Concanavalin A-binding glycopeptides from rat brain glycoproteins.
Hof HI, Susz JP, Javaid JI, Brunngraber EG.
The affinity of concanavalin A for neutral and acidic glycopeptides derived from
rat brain glycoproteins was investigated by studying the inhibition of a
concanavalin A-glycogen precipitation system. The neutral, mannose-rich
glycopeptides obtained by column electrophoresis of the dialyzable glycopeptides
that had been solubilized by proteolytic treatment of defatted brain tissue were
powerful inhibitors, with an inhibitory activity 20 to 26 times that of the
standard inhibitor, methyl-alpha-D-mannoside. The acidic sialoglycopeptides had
activities one to nine times that of the mannoside. Therefore, both acid and
neutral glycopeptides were capable of interacting with concanavalin A. The
especially strong affinity of the neutral mannose-rich glycopeptides, however,
enabled their retention on concanavalin A-Sepharose and subsequent elution with
methyl-alpha-D-mannoside. This provided the means of separation of the acidic
sialoglycopeptides from the neutral, mannose-rich glycopeptides by affinity
chromatography. Glycopeptides that contain N-acetylgalactosamine are not retained
by concanavalin A-Sepharose.
PMID: 1690 [Indexed for MEDLINE]