[Different character of zinc ion binding with lactate dehydrogenase M4 in diluted and concentrated solutions].
The study of the melting characteristics of lactate dehydrogenase M4 and Zn/lactate dehydrogenase at pH 6.5-8.5 by microcalorimetric methods shows that in dilute solutions of the enzyme (0.05% lactate dehydrogenase solution) one Zn ion causes destabilisation of enzyme structure, attended by a decrease of melting temperature throughout the entire pH interval under study. Concentrated solutions of the enzyme (0.4% lactate dehydrogenase solution) are a seat of such conformational changes of the latter which affect the character of Zn ions binding depending on pH.
Kiladze
A A
AA
Birkaia
V G
VG
Lomidze
E S
ES
Monaselidze
D R
DR
D000818:Animals; D002151:Calorimetry; D002412:Cations; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase / Q000737:chemistry / Q000378:metabolism*; D009994:Osmolar Concentration; D011485:Protein Binding; D011487:Protein Conformation; D012996:Solutions; D013552:Swine; D013696:Temperature; D015032:Zinc / Q000378:metabolism*
D002412:Cations; D007527:Isoenzymes; D012996:Solutions; D007770:L-Lactate Dehydrogenase; D015032:Zinc
Razlichnyĭ kharakter sviazyvaniia ionov tsinka s laktatdegidrogenazoĭM4 v razbavlennykh i kontsentrirovannykh rastvorakh.