Further biochemical data on Qa-2 |
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Authors: | James Michaelson Lorraine Flaherty Yuri Bushkin Holly Yudkowitz |
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Affiliation: | (1) Irvington House Institute, Department of Pathology, New York University Medical Center, 550 First Avenue, 10016 New York, New York;(2) New York State Department of Health, The Division of Laboratories and Research, 12201 Albany, New York;(3) Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, 10021 New York, New York |
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Abstract: | The Qa-2 differentiation alloantigen is coded by a gene situated between the D and Tla loci of the murine major histocompatibility complex (H-2). Qa-2-bearing protein was isolated by immunoprecipitation and found to be composed of subunits of 40 000 and 12 000 daltons by SDS polyacrylamide gel electrophoresis (PAGE). The 12 000 dalton material was identified as 2-microglobulin (2M) by its molecular weight (SDS PAGE), charge (isoelectric focusing), antigenicity (reactivity with xenogenic anti- 2M), and genetics. The 40 000 dalton mol. wt. of Qa-2 heavy chain is 5 000 daltons less than that of D and K molecules (45 000 daltons). The quantity of Qa-2 isolated by immunoprecipitation was found to vary in a strain-specific fashion and as much as a 15-fold difference was observed.Abbreviations used in this paper B6 C57BL/6 strain mice - B10 C57BL/10 mice - 2M beta 2-microglobulin - IEF isoelectric focusing - K 1000 daltons - MHC major histocompatibility complex - PAGE polyacrylamide gel electrophoresis - SDS sodium dodecyl sulfate - TL thymusleukemia antigen |
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