Premium
Interaction of Polyelectrolytes with Proteins, 3
Author(s) -
Shalova Iri.,
Naletova Iri.,
Saso Luciano,
Muronetz Vladimir I.,
Izumrudov Vladimir A.
Publication year - 2007
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200700052
Subject(s) - chemistry , polyelectrolyte , alkyl , alkylation , substituent , polymer chemistry , medicinal chemistry , chloride , sodium , methylene , enzyme , stereochemistry , organic chemistry , polymer , catalysis
The ability of quaternized polyamines (poly‐ N ‐alkyl‐4‐vinylpyridinium bromides possessing a number, m , of methylene groups in the N ‐alkyl substituent or a degree of alkylation, β , and n , n ‐ionene bromides) to suppress the thermoaggregation of glyceraldehyde‐3‐phosphate dehydrogenase increased in the order m = 1 < 3 < 5, β = 95 < 85 < 70 $\ll$ 45 < 35 < 20 and n = 3 < 6 < 10, which agrees well with the increase, in the same order, in the hydrophobicity of the chains. Complexing suppressed thermoaggregation, but not thermodenaturation of the enzyme, which was even encouraged by the polycations and occurred at room temperature when the most efficient suppressor (with β = 20) was used. The adverse effect was reduced by the addition of sodium chloride which destroyed the complex and resulted in a noticeable reactivation.