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Comparative Studies of Mouse (H-2) and Human (HL-A) Histocompatibility Antigens
- Source :
- European Journal of Biochemistry. 43:471-477
- Publication Year :
- 1974
- Publisher :
- Wiley, 1974.
-
Abstract
- A purification procedure applied to H-2 antigens (controlled by the H-2 locus) was used for the characterization of HL-A substances (HL-A2 and HL-A7) (controlled by the HL-A locus) solubilized from lymphoid cell membranes by delipidation. Upon Sephadex chromatography the serologically active material had an apparent Mr of 32000, and displayed, in relation to H-2 antigens, a faster electrophoretic mobility and higher pI values. One sulfhydryl group and one (intrachain) disulfide bond were present in partially purified HL-A preparations. Reduction and aminoethylation in 4 M urea did not influence the electrophoretic migration of HL-A active substances, suggesting that, as already demonstrated for H-2 alloantigens, in HL-A molecules the genetic determinants are present on single polypeptide chains. Highly purified HL-A alloantigens, like H-2 substances, revealed a high degree of microheterogeneity. These findings further support the concept of the genetic and structural homology of the main histocompatibility systems in mouse and man.
- Subjects :
- Alkylation
Cell
Locus (genetics)
Biology
Biochemistry
Cell Line
Mice
Species Specificity
Antigen
Histocompatibility Antigens
medicine
Pi
Animals
Electrophoresis, Paper
Disulfides
Lymphocytes
Chromatography, Ion Exchange
Electrophoresis, Disc
Molecular biology
Histocompatibility
Molecular Weight
Electrophoresis
medicine.anatomical_structure
Membrane
Sephadex
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Oxidation-Reduction
Subjects
Details
- ISSN :
- 14321033 and 00142956
- Volume :
- 43
- Database :
- OpenAIRE
- Journal :
- European Journal of Biochemistry
- Accession number :
- edsair.doi.dedup.....82c9b6a455d6c435eed0905ede621dcc