Purification and characterization of human lysosomal membrane glycoproteins.

@article{Mane1989PurificationAC,
  title={Purification and characterization of human lysosomal membrane glycoproteins.},
  author={S M Mane and Louis Marzella and Dorothy Ford Bainton and V K Holt and Y. -N. Cha and James E. K. Hildreth and J. Thomas August},
  journal={Archives of biochemistry and biophysics},
  year={1989},
  volume={268 1},
  pages={360-78}
}
Two human cell lysosomal membrane glycoproteins of approximately 120 kDa, hLAMP-1 and hLAMP-2, were identified by use of monoclonal antibodies prepared against U937 myelomonocytic leukemia cells or blood mononuclear cells. The two glycoproteins were purified by antibody affinity chromatography and each was found to be a major constituent of human spleen cells, representing approximately 0.05% of the total detergent-extractable protein. Both molecules were highly glycosylated, being synthesized… CONTINUE READING

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