Affinity Electrophoresis Used for Analses on the Interactions Between Dehydrogenases and Their Cofactors
山口医学 Volume 34 Issue 2
Page 85-92
published_at 1985-04
Title
Affinity電気泳動法による脱水素酵素-補酵素結合反応の解析
Affinity Electrophoresis Used for Analses on the Interactions Between Dehydrogenases and Their Cofactors
Source Identifiers
Analyses on the interactions between dehydrogenases and their cofactors by utilizing affinity electrophoresis (AEP) technique are described. Dissociation constants of NAD-dependent dehydrogenases (NAD-DH) and NADP-dependent dehydrogenases (NADP-DH) for cofactor analogues, 5'-AMP and 2'AMP, were determined by AEP. A comparison of those dissociation constants suggests :(a) NAD-DH and NADP-DH from different sources have diverse affinities to 5'-AMP and 2'-AMP, (b) a phosphate group at position of 2' in ribose moiety of 2'-AMP and NADP play an important role in the cofactor binding onto NADP-DH, (c) lactate dehydrogenase (LDH) isozymes which have more M subunits (skeletale muscle type subunit) in their tetrameric structure have the stronger affinity to 5'AMP. From these observations, it will be concluded that AEP is useful not only for separation of enzymes according to their biological activities but also for analysis of the effect of subunits interaction on the cofactor binging to enzymes which have different types of subunit in oligomeric structure.
Languages
jpn
Resource Type
journal article
Publishers
山口大学医学会
Date Issued
1985-04
File Version
Not Applicable (or Unknown)
Access Rights
metadata only access
Relations
[ISSN]0513-1731
[NCID]AN00243156
Schools
医学部