| Project/Area Number |
02680140
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
物質生物化学
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| Research Institution | Faculty of Pharmaceutical Sciences, Teikyo University |
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Principal Investigator |
KASAI ken-ichi Teikyo Univ., Fac. Pharm. Sci., Professor, 薬学部, 教授 (40001052)
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| Co-Investigator(Kenkyū-buntansha) |
HIRABAYASHI Jun Teikyo Univ., Fac. Pharm. Sci., Assistant Professor, 薬学部, 助手 (40156691)
OHYAMA Yuji Teikyo Univ., Fac. Pharm. Sci., Assistant Professor, 薬学部, 助手 (90129982)
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| Project Period (FY) |
1990 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1991: ¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 1990: ¥1,100,000 (Direct Cost: ¥1,100,000)
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| Keywords | animal lectin / galactoside-binding lectin / human lectin / chicken lectin / cDNA cloning / recombinant protein / site-directed mutagenesis / ガラクトシド総合レクチン / cDNAリロ-ニング / 組換たんぱく質 |
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| Research Abstract |
Metal-independent beta-galactoside-binding lectins of vertebrates are considered to be involved a variety of important biological regulations such as development of embryo and morphogenesis of tissues in which specific interaction between complex carbohydrates and their counterparts play crucial roles. They are also suggested to be involved in regulation of immune system and metastasis of malignant cells. In the present research, complete amino acid sequence, complete nucleotide sequence of cDNA, expression of recombinant protein in E. coli and the fate during development of embryo of one of chicken isolectin, i. e., 16 kDa lectin, were elucidated. The results made it possible to understand its roles during morphogenesis of various tissues especially that of skin, and also molecular evolution of this lectin family. Effects of substitution of amino acid residues by site-directed mutagenesis of recombinant human 14 kDa lectin showed that a tryptophan and some cystein residues which had been considered to be mostly important were not essential for carbohydrate binding. A cDNA for another human lectin, 29 kDa lectin, was cloned from a library derived from a breast carcinoma. Complete amino acid sequence of a lectin contained in venom of Crotalus was determined in order to know whether it belongs to the metal-independent lectin family or not. The result clearly showed that the snake venom lectin is a member of calcium-dependent lectin family.
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