| Project/Area Number |
02670717
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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 |
Urology
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| Research Institution | Saitama Medical School |
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Principal Investigator |
YOSHIDA Ken-ichiro Saitama Medical School, Urology, Associate prof., 医学部, 助教授 (00134685)
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| Project Period (FY) |
1990 – 1992
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| Project Status |
Completed (Fiscal Year 1992)
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| Budget Amount *help |
¥2,600,000 (Direct Cost: ¥2,600,000)
Fiscal Year 1992: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1991: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1990: ¥1,600,000 (Direct Cost: ¥1,600,000)
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| Keywords | NAG isoenzymes / enzymatic properties / human reproductive organs / human renal tissues / human renal cell carcinomas / hexosaminidase C / sugar-chain structures / Hexosaminidase C / NAG A / 腎細胞癌 / NAG / ヒト精巣 / ヒト精漿 / ヒト前立腺肥大症組織 / レクチンアフィニティーカラム / ヒト腎 / 精製 |
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| Research Abstract |
N-acetyl-beta, D-glucosaminidases(NAGs) from human seminal plasma, testes and renal tissues were purified and those of enzymatic properties, such as molecular weight (MW), kinetic studies and sugar-chain structures were studied. The MW of NAGs from different origins showed similar value(140kDa), while inhibition studies by Ba^<2+> and Zn^<2+> for NAGs showed different results between reproductive and renal tissue origins. The sugar-chain studies of NAGs using Con A and WGA lectin columns revealed that there were no significant difference between the two origins. Isoenzyme B was higher in the reproductive origins, while isoenzyme A was higher in the renal origin.
The NAG A purified from human testes and renal tissues, was studies on the enzymatic properties and the sugar-chain structures. The enzymatic properties including MW were similar between the testes and the renal origins. Both NAG A were revealed possessing a little amount of complex sugar-chains, which was higher in the testes origin than the renal one.
Hexosaminidase C from human renal tissues was demonstrated and its enzymatic properties were studied. The enzymatic properties of NAG A obtained from human renal cell carcinoma tissues were compared with those of the normal tissues, resulting that there were no significant differences in the catalytic properties while the sugar-chain structures were different ; the complex type and the hybrid type with fucose residue were significant higher while the high mannose type and the hybrid type without fucose residue were significant lower in the carcinoma origin.
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