Feb 13, 1976

The sulphatase of ox liver. XIX. On the nature of the polymeric forms of sulphatase A present in dilute solutions

Biochimica Et Biophysica Acta
A JerfyH J Tomkins

Abstract

Weight-average elution volumes of sulphatase A (an arylsulphate sulphohydrolase, EC 3.1.6.1) from Sephadex G-200 have been determined as functions of protein concentration, pH, ionic strength and temperature. The results are used to calculate the apparent association equilibrium constants for tetramer formation and the associated standard-state thermodynamic parameters. While the apparent association constant decreased from 10(28) to 10(21) M-3 on increasing the pH from 4.5 to 5.6 at ionic strength 0.1, at any particular pH value studied it was relatively insensitive to temperature variation so that deltaH is close to zero and tetramer formation in solution is associated with a positive entropy change. At pH 5.0, increasing the ionic strength from 0.1 to 2 decreased the association constant by a factor of 100. Methylumbelliferone sulphate has no effect on the association of sulphatase A. The equilibrium results are used to define the degree of association of sulphatase A likely to encountered in experiments designed to elucidate its kinetic properties. In the liver lysosome, the tetramer is probably the dominant species. The monomer and tetramer of sulphatase A have similar, or identical, specific activities with nitrocatechol ...Continue Reading

Mentioned in this Paper

Thermodynamics
Macromolecular Compounds
Sephadex G 200
Lysosome Assembly Pathway
Deoxycholic Acid, Monoammonium Salt
Sodium Taurodeoxycholate
Aggregation
Manganese chloride
Lysosomes
Polymers

About this Paper

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