2024-03-29T14:18:37Z
https://nagoya.repo.nii.ac.jp/oai
oai:nagoya.repo.nii.ac.jp:02005197
2023-03-27T02:07:51Z
1213:1620:1621:1679636128616
Determination of α-Ketoisocaproate Dioxygenase Activity in Mammalian Livers
Xu, Ming
Nagasaki, Masaru
Li, Zhihao
Obayashi, Mariko
Baggiotto, Gustavo
Sato, Yuzo
Shimomura, Yoshiharu
The α-ketoisocaproate dioxygenase (KICD) catalyzes the decarboxylation of α-ketoisocaproate (KIC). derived from transamination of leucine, to β-hydroxy-β-methylbutyrate (HMB) in the cytosol of the liver. The characterization of the purified KICD from rat and human livers indicated that this enzyme requires Fe^2+ for its activity, but does not use CoA-SH and NAD^+ as cofactors that are required for the branched-chain α-keto acid dehydrogenase complex (BCKDC), which catalyzes the decarboxylation of KIC to isovalery-CoA in mitochondria. In the present study, a radiochemical assay was developed to measure the KICD activity in liver extracts. In this method, the decarboxylation of KIC by BCKDC was eliminated by addition of BCKDC-antiserum in the assay mixture. Evidence is provided here for establishment of improved assay conditions for KICD in liver extracts.
departmental bulletin paper
名古屋大学総合保健体育科学センター
The Research Center of Health, Physical Fitness and Sports, Nagoya University
2002-03-29
application/pdf
総合保健体育科学
1
25
7
11
Nagoya Journal of Health, Physical Fitness & Sports
0289-5412
https://nagoya.repo.nii.ac.jp/record/2005197/files/njhpfs_25_1_7.pdf
jpn