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> 생화학분자생물학회 > BMB Reports > 32권 5호

Chemical Modification of Brain Glutamate Dehydrogenase Isoproteins with Phenylglyoxal

Chemical Modification of Brain Glutamate Dehydrogenase Isoproteins with Phenylglyoxal

(Jee Yin Ahn) , (Eun Hee Cho) , (Kil Soo Lee) , (Soo Young Choi) , (Sung Woo Cho)

- 발행기관 : 생화학분자생물학회

- 발행년도 : 1999

- 간행물 : BMB Reports, 32권 5호

- 페이지 : pp.515-520 ( 총 6 페이지 )


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논문제목
초록(외국어)
Incubation of two types of glutamate dehydrogenase isoproteins from bovine brain with the arginine-specific dicarbonyl reagent phenylglyoxal resulted in a biphasic loss of enzyme activity. Reaction of the glutamate dehydrogenase isoproteins with phenylglyoxal caused a rapid loss of 53∼62% of the enzyme activities and modification of two residues of arginine per enzyme subunit. Prolonged incubation of the glutamate dehydrogenase isoproteins with phenylglyoxal resulted in the modification of an additional four residues of arginine per enzyme subunit without further loss of the residual activities. Partial protection against inactivation was provided by the coenzyme NADH or substrate 2-oxoglutarate. The most marked decrease in the rate of inactivation was observed by the combined addition of NADH and 2-oxoglutarate, suggesting that the first two modified arginine residues are in the vicinity of the catalytic site. However, inactivation of the glutamate dehydrogenase isoproteins by phenylglyoxal appears to be partial with approximately 40 % activity remained after an extended reaction time with excess reagent, suggesting that the modified arginine residues may not be directly involved in catalysis. The lack of complete protection by substrates also suggest the possibility that the modified arginine residues are not directly involved at the active site, and the partial loss of activity by the modification of arginine residues may be due to a conformational change. There were no significant differences between the two glutamate dehydrogenase isoproteins in sensitivities to inactivation by phenylglyoxal, indicatingthat the microenvironmental structures of the glutamate dehydrogenase isoproteins are very similar to each other.

논문정보
  • - 주제 : 자연과학분야 > 화학
  • - 발행기관 : 생화학분자생물학회
  • - 간행물 : BMB Reports, 32권 5호
  • - 발행년도 : 1999
  • - 페이지 : pp.515-520 ( 총 6 페이지 )
  • - UCI(KEPA) : I410-ECN-0102-2009-470-007262640
저널정보
  • - 주제 : 자연과학분야 > 화학
  • - 성격 : 학술지
  • - 간기 : 월간
  • - 국내 등재 : KCI 등재
  • - 해외 등재 : - / SCOPUS
  • - ISSN : 1976-6696
  • - 수록범위 : 1968–2022
  • - 수록 논문수 : 4632