The Comparative Study of the Interaction of Yeast and Horse Liver Alcohol Dehydrogenases with Reactive Dyes by Affinity Partitioning in Two-Phase Systems-Reference-Cited by-同舟云学术

The Comparative Study of the Interaction of Yeast and Horse Liver Alcohol Dehydrogenases with Reactive Dyes by Affinity Partitioning in Two-Phase Systems

Published:1989 Issue: Volume: Page:175-189
ISSN:
Container-title:Protein-Dye Interactions: Developments and Applications
language:
Short-container-title:

Author:

Pesliakas J.-H. J.,Zutautas V. V.,Glemza A. A.

Publisher

Springer Netherlands

Link

http://link.springer.com/content/pdf/10.1007/978-94-009-1107-9_19.pdf

Reference9 articles.

1. Plaksaite S.S., Sudzhuviene O.F., Pesliakas J.-H.J., Glemzha A.A. Role of metal ions in specific binding of yeast alcohol dehydrogenase by free dyes and dye-adsorbents. Bioorg. Khimiya, 1984, v.10, No1, p.25–31.

2. Plaksaite S.S., Sudzhuviene O.F., Pesliakas J.-H.J., Glemzha A.A. Group specific adsorbents with immobilized dyes for purification of the yeast alcohol dehydrogenase. Prikladnaya Biokhim. Mikrobiol., 1985, v.21, iss1, p.25–34.

3. Flaksaite S.S., Sudzhuviene O.F., Pesliakas J.-H.J., Glemzha A.A. Role of metal ions to specific binding of yeast alcohol dehydrogenase by free and immobilized dyes. Inorgan. Chim. Acta, 1983, v.79, p.157–158.

4. Plaksaite S.S., Sudzhuviene O.F., Pesliakas J.-H.J., Glemzha A.A. The interaction between dyes-Cu(II) complexes with the yeast alcohol dehydrogenase. The possibility of the involvment of the histidine residue of the enzyme in the formation of a mixed Cu(II)-complex with light-resistant yellow 2KT. Biorg. Khimiya, 1987, v.13, No3, p.293–299.

5. Flaksaite S.S., Sudzhuviene O.F., Pesliakas J.-H.J., Glemzha A.A., Studies on the interaction of EAD(H)-dependent dehydrogenases with reactive dyes and their transient metal ion complexes. Biokhimiyat, 1987, v.52, iss1, p.73–81.