NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.

@article{Weisshaar1991NMRIO,
  title={NMR investigations of the N-linked oligosaccharides at individual glycosylation sites of human lutropin.},
  author={G Weisshaar and J Hiyama and Andrew G. Renwick and Manfred Nimtz},
  journal={European journal of biochemistry},
  year={1991},
  volume={195 1},
  pages={257-68}
}
Human lutropin or luteinizing hormone (hLH) is a heterodimeric glycoprotein, composed of two subunits. hLH alpha (N-glycosylated at Asn52 and Asn78) and hLH beta (N-glycosylated at Asn30). The sugar chains were liberated by hydrazinolysis from intact hLH beta and from glycopeptides obtained after tryptic digestion of hLH alpha, subsequently reduced and fractionated as alditols by anion-exchange and ion-suppression amine-adsorption HPLC and identified mainly by one-dimensional (1D) and two… CONTINUE READING

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