Structural polymorphism of mouse complement C2 detected by microscale peptide mapping: Linkage to H-2 |
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| Authors: | Sei Takahashi Yoshihiro Fukuoka Kazuo Moriwaki Tomoko Okuda Takehiko Tachibana Shunnosuke Natsuume-Sakai Morinobu Takahashi MD |
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| Institution: | (1) The Department of Immunobiology, Cancer Research Institute, Kanazawa University, 920 Kanazawa, Japan;(2) The Department of Immunology, the Institute of Tuberculosis and Cancer, Tohoku University, 980 Sendai, Japan;(3) The Department of Cytogenetics, the National Institute of Genetics, 411 Mishima, Japan;(4) Department of Immunobiology, Cancer Research Institute, Kanazawa University, 13-1 Takaramachi, 920 Kanazawa, Japan |
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| Abstract: | Complement C2 was isolated from 17 mouse strains by immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis and examined for structural polymorphism by using micro-peptide mapping. By comparing the peptide maps of tryptic digests of C2 from various strains, two allotypic variations were detected. B 10 and 14 other mouse strains demonstrated C2.1 type, while a wild mouse line (M.Mol-Ohm) and one BIO congenic strain, B10.MOL.OHM, which carries the H-2 derived from M.Mol-Ohm, demonstrated C2.2 type. (B10 × Bl0.MOL.OHM)F1 demonstrated codominantly expressed C2 type (C2.1.2). Desialation of mouse C2 did not abolish the observed variation of mouse C2. It is concluded that an H-2-linked codominant locus controls the structure of mouse complement C2, further confirming the extensive homology of the major histocompatibility complex among higher vertebrate species. |
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