Abstract:A structural glycopeptide, gp4l, derived from the occluded virus of the baculovirus Autographa californica nuclear polyhedrosis virus was characterized. The peptide specifically bound wheat germ agglutinin but was not recognized by a panel of seven other lectins. Reactivity with wheat germ agglutinin was eliminated by treatment of gp4l with beta-N-acetylglucosaminidase, indicating that N-acetylglucosamine (GlcNAc) was
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