Effect of poly(phosphate) anions on glyceraldehyde-3-phosphate dehydrogenase structure and thermal aggregation: comparison with influence of poly(sulfoanions)

• Published in: Biochimica et biophysica acta Vol. 1830; no. 10; pp. 4800 - 4805
• Main Authors: Semenyuk, Pavel I., Muronetz, Vladimir I., Haertlé, Thomas, Izumrudov, Vladimir A.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2013; Elsevier
• Subjects: Anions; calorimetry; Calorimetry - methods; Chemical and Process Engineering; dextran; Dextran sulfate; dextrans; differential scanning calorimetry; Engineering Sciences; enzymatic activity; enzyme activity; Food engineering; glyceraldehyde-3-phosphate dehydrogenase; Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry; Life Sciences; Particle Size; phosphates; Poly(styrenesulfonate); Polyanions; polymerization; polymers; Polyphosphate; Polyphosphates - chemistry; post-translational modification; Protein aggregation; Protein Conformation; protein structure; Protein sulfation; proteins; sulfates; Temperature; thermal stability; titration; turbidity; Protein aggregation; Polyanions; Polyphosphate; DSC; Poly(styrenesulfonate); DSx; Dextran sulfate; PPx; PSSx; GAPDH; Protein sulfation; dextran sulfate containing x charged groups per molecule; poly(styrenesulfonate) with the degree of polymerization x; DS(x); PSS(x); PP(x); differential scanning calorimetry; glyceraldehyde-3-phosphate dehydrogenase; poly(phosphate) with the degree of polymerization x; AMINO-TERMINUS; TYROSINE O-SULFATION; COMPLEXES; THERMOAGGREGATION; PURIFICATION; HIV-1 ENTRY; OLIGOMERIC ENZYMES; PROTEINS; POSTTRANSLATIONAL MODIFICATION

It is well documented that poly(sulfate) and poly(sulfonate) anions suppress protein thermal aggregation much more efficiently than poly(carboxylic) anions, but as a rule, they denature protein molecules. In this work, a polymer of different nature, i.e. poly(phosphate) anion (PP) was used to elucid...