Binding of arylsulphatase Β to isolated rat liver lysosomal membranes.
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Date
1981-09
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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.
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Keywords
Rat liver, lysosomal membrane, arylsulphatase Β, arylsulphatase B lysosomal membrane complex, dissociation, sialic acid
Citation
Adhikari H R, Ahmed Ateeq, Vakil U K. Binding of arylsulphatase Β to isolated rat liver lysosomal membranes. Journal of Biosciences. 1981 Sept; 3(3): 285-292.