Purification of HLA-linked B lymphocyte alloantigens in immunologically active form by preparative sodium dodecyl sulfate-gel electrophoresis and studies on their subunit association.

作者：T. A. Springer, Jim Kaufman, Lyle A. Siddoway, Dean L. Mann, Jack L. Strominger · 发表于：Journal of Biological Chemistry · 年份：1977 · DOI：10.1016/s0021-9258(17)40050-0 · 被引用次数：79 · 研究领域：Photoreceptor and optogenetics research、Nicotinic Acetylcholine Receptors Study、Lipid Membrane Structure and Behavior

The HLA-linked B cell alloantigen (p29,34) is composed of two subunits of 29,000 (p29) and 34,000 (p34) molecular weight. The partially purified HLA-linked B cell alloantigen was purified by a final step of preparative sodium dodecyl sulfate-gel electrophoresis. An antiserum was prepared against p29,34 which specifically lysed B lymphocytes. In sodium dodecyl sulfate at 21 degrees, p29 and p34 remained noncovalently associated and retained immunologic activity; subunit dissociation at higher temperatures correlated with loss of immunologic activity. Although the pI values of p29 and p34 are 6.1 and 5.2, respectively, the subunits co-electrofocus under nondenaturing conditions. In addition, cross-linking studies showed the B cell antigen has a (p29)1(p34)1 subunit structure.