Human neutrophil plasma membrane. Specific labelling, topological distribution of proteins and surface antigen detection

Pedro Lacal, Faustino Mollinedo, Vicente Larraga

Research output: Contribution to journalArticle

Abstract

We describe here the major protein components of a highly purified human neutrophil plasma membrane fraction analyzed by uni- and two-dimensional gel electrophoresis, as well as their glycoprotein nature as determined by PAS staining, [125I]-Con A binding and [3H]-sodium borohydride labelling. A polypeptide of about 150kDa appeared as the main Con A binding protein. The topology of the polypeptides has also been determined by protein labelling from the outside of the cell surface by lactoperoxidase catalyzed iodination and from within the bilayer by using the hydrophobic reagent [1251]-iodonaphtylazide. The antigenic features of some cell surface polypeptides have also been determined by the use of monoclonal antibodies. In this context we have detected by immunoprecipitation in human neutrophils the antigen MAC 120, previously found in monocytes and putatively associated with antigen presenting function.

Original languageEnglish
Pages (from-to)161-171
Number of pages11
JournalMolecular and Cellular Biochemistry
Volume77
Issue number2
DOIs
Publication statusPublished - Oct 1987

Keywords

  • cell surface antigens
  • glycoproteins
  • neutrophils
  • plasma membrane protein

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology

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