Binding of arylsulphatase Β to isolated rat liver lysosomal membranes.

ABSTRACT

Binding of arylsulphatase Β to isolated rat liver lysosomal membrane has been studied at 37°C. The binding is strongly pH dependent and is governed by ionic strength of the medium. Experimental evidence is given for the ability of the enzyme to dissociate from the firmly formed membrane enzyme complex. The dissociation rate is greatly accelerated by raising the buffer molarity. Neuraminidase treatment of the membrane causes significant reduction in its binding ability to the enzyme. This suggests that sialic acid groups participate, presumably by maintaining surface negativity of the membrane, at a stage of enzyme membrane interaction process which precedes the internalization of the lysosomal enzymes in the lyso omes.