Ly-6A.2 and Ly-6E.1 molecules are antithetical and identical to MALA-1 Journal Article


Authors: Palfree, R. G. E.; Dumont, F. J.; Hammerling, U.
Article Title: Ly-6A.2 and Ly-6E.1 molecules are antithetical and identical to MALA-1
Abstract: Rat monoclonal antibodies YE3/19.1, defining the murine-activated lymphocyte antigen MALA-1, and D7, detecting an Ly-6 locus-controlled antigen, bound highly purified Ly-6E.1. On western blots of lymphocyte surface proteins which had been solubilized and electrophoretically separated in octylglucoside, they detected bands which comigrated with Ly-6A.2 or Ly-6E.1 antigens. On cells or in an immunoassay they blocked alloantibodies against Ly-6A.2 or Ly-6E.1. The tissue distribution of MALA-1 also correlated with Ly-6A.2 or Ly-6E.1. Upon octylglucoside or sodium dodecyl sulfate-polyacrylamide gel electrophoresis, these antigens displayed similar sizes. Thus, Ly-6A.2 and Ly-6E.1 are most likely products of alternate alleles. Electrophoretic analysis showed a similar size and charge for Ly-6A.2, Ly-6B.2, Ly-613.2, and Ly-27.2. Ly-6C.2 and Ly-28.2 appeared to be identical, and were similar in size to Ly-6A.2, but they differed in charge and in intrachain disulfide constraints. Since Ly-613.2 and Ly-27.2 may represent the same or different epitopes on the Ly-6A.2 molecule, the previously postulated five Ly-6-like antigens that were thought to be separable on the basis of tissue distribution, may represent no more than three separate proteins which can be assigned to one of two distinct categories by electrophoretic mobility in gels containing octylglucoside. © 1986 Springer-Verlag.
Keywords: comparative study; mouse; animal; mice; membrane antigen; antibodies, monoclonal; antibody specificity; rats; enzyme-linked immunosorbent assay; lymphocytes; antigens, ly; ly antigen; electrophoresis; electrophoresis, polyacrylamide gel; priority journal; isoantibodies; support, u.s. gov't, p.h.s.; glucosides
Journal Title: Immunogenetics
Volume: 23
Issue: 3
ISSN: 0093-7711
Publisher: Springer  
Date Published: 1986-03-01
Start Page: 197
End Page: 207
Language: English
DOI: 10.1007/bf00373821
PUBMED: 3957415
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 18 August 2021 -- Source: Scopus
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  1. Roger G. E. Palfree
    17 Palfree