Isolation and characterization of plasma membrane associated immunoglobulin from cultured human diploid lymphocytes

Stephen Kennel, Richard A. Lerner

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

The lactoperoxidase iodination method was adapted to label surface proteins of cultured diploid human lymphocytes. Membrane associated immunoglobulin of the μ,K type was isolated from WIL2-A3 cells as well as from their purified membrane preparations by detergent solubilization of labeled membrane proteins and subsequent precipitation with specific antisera. These data indicate that using our conditions all of the labeled immunoglobulin was membrane bound. The molecular weight of the bound molecule was estimated to be 265,000±15,800 by sodium dodecyl sulfate gel electrophoresis and on reduction was separated into proteins with molecular sizes identical to μ and light-chain markers. The combination of two μ and two light chains to give an "IgM monomer" configuration should give a molecular weight of 180,000 to 200,000. Possible reasons for this discrepancy are discussed.

Original languageEnglish (US)
JournalJournal of Molecular Biology
Volume76
Issue number4
DOIs
StatePublished - Jun 5 1973

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Diploidy
Immunoglobulins
Membrane Proteins
Molecular Weight
Cell Membrane
Lymphocytes
Lactoperoxidase
Light
B-Cell Antigen Receptors
Membranes
Halogenation
Sodium Dodecyl Sulfate
Detergents
Immunoglobulin M
Electrophoresis
Immune Sera
Gels
Proteins

All Science Journal Classification (ASJC) codes

  • Molecular Biology

Cite this

Isolation and characterization of plasma membrane associated immunoglobulin from cultured human diploid lymphocytes. / Kennel, Stephen; Lerner, Richard A.

In: Journal of Molecular Biology, Vol. 76, No. 4, 05.06.1973.

Research output: Contribution to journalArticle

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