Interaction of polyelectrolytes with proteins, 3. Influence of complexing polycations on the thermoaggregation of oligomeric enzymes.
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, beta, and n,n-ionene bromides) to suppress the thermoaggregation of glyceraldehyde-3-phosphate dehydrogenase increased in the order m = 1 < 3 < 5, beta = 95 < 85 < 70 << 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 beta = 20) was used. The adverse effect was reduced by the addition of sodium chloride which destroyed the complex and resulted in a noticeable reactivation.
Shalova
Irina N
IN
School of Bioengineering and Bioinformatics, Lomonosov Moscow State University, Leninskie Gory, Moscow, 119992, Russia.
Naletova
Irina N
IN
Saso
Luciano
L
Muronetz
Vladimir I
VI
Izumrudov
Vladimir A
VA
D019281:Dimerization; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D011073:Polyamines / Q000737:chemistry*; D000071228:Polyelectrolytes; D011489:Protein Denaturation; D012965:Sodium Chloride; D013696:Temperature
D004798:Enzymes; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D011073:Polyamines; D000071228:Polyelectrolytes; D012965:Sodium Chloride