Successive Purification of Several Enzymes Having Affinities for Phosphoric Groups of Substrates by Affinity Chromatography on P-Cellulose1

Autor:	Isamu Takagahara, Suzuki Yasuo, Tuyosi Fujita, Takekazu Horio, Jun-iti Yamauti, Fujii Katsumi, Jinpei Yamashita
Rok vydání:	1978
Předmět:	chemistry.chemical_classification Chromatography Chemistry Elution Glutathione reductase Dehydrogenase General Medicine Biochemistry Yeast chemistry.chemical_compound Enzyme Affinity chromatography Cellulose Molecular Biology Pyruvate kinase
Zdroj:	The Journal of Biochemistry. 83:585-597
ISSN:	1756-2651 0021-924X
DOI:	10.1093/oxfordjournals.jbchem.a131946
Popis:	Glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, glutathione reductase and pyruvate kinase of Candida utilis and baker's yeast, when in anionic form, were adsorbed on a cation exchanger, P-cellulose, due to affinities similar to those for the phosphoric groups of their respective substrates; thus, glucose-6-phosphate dehydrogenase was readily eluted by either NADP+ or NADPH, glutathione reductase by NADPH, 6-phosphogluconate dehydrogenase by 6-phosphogluconate, and pyruvate kinase by either ATP or ADP. This type of chromatography may be called "affinity-adsorption-elution chromatography"; the main principle is different from that of so-called affinity-elution chromatography. Based on these findings, a large-scale procedure suitable for successive purification of several enzymes having affinities for the phosphoric groups of their substrates was devised. As an example, glucose-6-phosphate dehydrogenase was highly purified from baker's yeast and crystallized.
Databáze:	OpenAIRE
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