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Catalytic influence of heparin on auramine O hydrolysis: A basis for differentiating heparin from other glycosaminoglycans based on its properties as a polyelectrolyte
Author(s) -
Band Philip,
Lukton Aaron
Publication year - 1984
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360231109
Subject(s) - chemistry , polyelectrolyte , counterion , hydronium , heparin , ionic strength , counterion condensation , catalysis , sulfation , donnan potential , glycosaminoglycan , polymer , inorganic chemistry , ion , organic chemistry , aqueous solution , biochemistry , electrolyte , electrode
The basis for heparin's ability to accelerate the conversion of auramine O (AuO) to Michlers ketone [P. Band & A. Lukton (1982) Anal. Biochem. 120 , 19–24] is here explained in terms of well‐known polyelectrolyte phenomena. Acceleration of this acidcatalyzed hydrolysis appears to be due to colocalization of the cationic dye and hydronium ion within the microenvironment of heparin's electrostatic domain. The dependence of reaction rate on polymer, dye, and hydronium ion concentration, ionic strength, and various ratios of these parameters is consistent with what others have observed for polyelectrolyte catalysts. Dextran sulfate, polyvinyl sulfate, and polyanethole sulfonate likewise accelerate this reaction, thus precluding any explanation of the catalysis in terms of a specific catalytic site. A striking aspect about the polyanion–AuO system is the inability of all other natural glycosaminoglycans tested to catalyze this reaction, despite their analogous polyanionic nature. Manning's limiting laws describing counterion condensation in polyelectrolyte solutions provide a simple context within which to interpret these results. Calculation of the structural linear charge density parameter, ξ, based on analytically determined sulfate‐to‐hexosamine ratios, reveals that heparin is unique among the glycosaminoglycans in possessing an ξ value greater than unity under the conditions described. Thus, heparin's differential ability to catalyze AuO hydrolysis is a reflection of the fact that only heparin is sulfated to an extent great enough to maintain ξ > 1, even when the negative charge of carboxylate groups is neutralized. It is proposed that this distinction may be important to the unique biochemical attributes of heparin and that such considerations may prove useful in establishing structure–function relationships when comparing different glycosaminoglycan classes.