T Cell Recognition of β-Lactoglobulin(Biological Chemistry)
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概要
- 論文の詳細を見る
Identification of the T-cell recognition sites in β-lactoglobulin (β-LG), the major allergen in bovine milk, was attempted with its enzymatic digests. The peptides from both the tryptic and chymotryptic digests of reduced carboxymethylated (RCM) β-LG were separated by gel-filtration and reverse-phase HPLC. Co-culturing lymph node cells from β-LG-primed BALB/c mice with each fraction, T-cell proliferation was examined by uptake of ^3H-labelled-thymidine. Three tryptic fragments (the residues ^<21>Ssr-^<40>Arg, ^<41>Val-^<60>Lys, and ^<102>Tyr-^<124>Arg) and three chymotryptic fragments (the residues ^<21>Ser-^<32>Leu, ^<59>Gln-^<82>Phe, and ^<123>Val-^<140>Leu) could stimulate the proliferation of the T cells. There T-cell antigenic sites seem to be located on the surface regions of the β-LG molecule. They didn't agree completely with the T-cell epitopes of β-LG predicted by the amphipathic periodicity hypothesis.
- 社団法人日本農芸化学会の論文
- 1988-10-23
著者
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TAKAHASHI Takeshi
Department of Electrical and Electronic Engineering, Akita University
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YAMAUCHI Kunio
Department of Agricultural Chemistry, The University of Tokyo
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Ando Osamu
Department Of Agricultural Chemistry The University Of Tokyo
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Kuwata Tamotsu
Central Research Institute Meiji Milk Pruducts Co. Ltd.
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Kuwata Tamotsu
Central Research Institute Meiji Milk Products Co. Ltd.
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Yamauchi Kunio
Department Of Agricultural Chemistry The University Of Tokyo
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Takahashi T
Univ. Tokyo Tokyo Jpn
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KAMINOGAWA Shunichi
Department of Agricultural Chemistry, The University of Tokyo
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Kaminogawa S
Department Of Agricultural Chemistry The University Of Tokyo
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Takahashi Takeshi
Department Of Agricultural Chemistry The University Of Tokyo
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