Affinity Chromatography of a Group Specific Adsorbent for Pyridoxal Phosphate Dependent Enzymes(Biological Chemistry)
スポンサーリンク
概要
- 論文の詳細を見る
Sepharose gels with L-amino carboxylic acid residues as a ligand (L-adsorbent) or with D-amino carboxylic acid residues (o-adsorbent) were prepared and used in affinity chromatography. Among enzymes involved in the metabolism of glutamic acid, a group of pyridoxal phosphate dependent enzymes such as aspartate aminotransferase, alanine aminotransferase, and glutamate decarboxylase had significant affinity for the L-adsorbent, while glutamate dehydrogenase (an NADP dependent enzyme) had no detectable affinity for either the L-or the D-adsorbent. The affinity chromatography with L-adsorbent was used for the purification of serine hydroxymethyltransferase: a pyridoxal phosphate dependent enzyme.
- 社団法人日本農芸化学会の論文
- 1986-11-23
著者
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Masuda T
Gifu Pharmaceutical Univ. Gifu
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Masuda Toshiya
Laboratory Of Organic Chemistry Faculty Of Agriculture Nagoya University
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Tai Akira
Institute For Protein Research Osaka University
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Ozaki H
Ajinomoto Co. Ltd. Kanagawa Jpn
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Masuda T
Laboratory Of Food Chemistry Faculty Of Science Of Living Osaka City University
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MASUDA Tsutomu
Shitennoji International Buddhist University
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OZAKI Hiroshi
Institute for Protein Research, Osaka University
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