Purification and structural characterisation of human HLA-linked B-cell antigens
- 1 July 1977
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 268 (5617) , 213-218
- https://doi.org/10.1038/268213a0
Abstract
The human B [bone marrow-derived] cell-specific alloantigen which is closely linked genetically to HL-A contains 2 non-covalently associated, sialogycoprotein subunits of MW 29,000 (p29), and 34,000 (p34). Although p29 and p34 have different amino-terminal sequences, their tyrosine peptide maps indicate considerable similarity in other portions of their polypeptide chains. Thus the genes for their proteins may have evolved by duplication of a common ancestral gene. Another lymphocyte cell surface protein of MW 16,000 (p16) was also characterized. Both p16 and p44 (the H chain of HL-A-A,B antigens) were compared with p29 and p34.This publication has 31 references indexed in Scilit:
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