The binding requirements of monkey brain lysosomal enzymes to their immobilised receptor protein |
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Authors: | Keith Alvares K Panneerselvam A S Balasubramanian |
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Institution: | (1) Neurochemistry Laboratory, Department of Neurological Sciences, Christian Medical College Hospital, 632004 Vellore, India |
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Abstract: | The lysosomal enzyme binding protein (receptor protein) isolated from monkey brain was immobilised on Sepharose 4B and used
to study the binding of brain lysosomal enzymes. The immobilised protein could bind \-D-glucosaminidase, α-D-mannosidase,
α-L-fucosidase and2-D-glucuronidase. The bound enzymes could be eluted either at an acid pH of 4.5 or by mannose 6-phosphate
but not by a number of other sugars tested. Binding could be abolished by prior treatment of the lysosomal enzymes with sodium
periodate. Alkaline phosphatase treatment of the enzymes did not prevent the binding of the lysosomal enzymes to the column
but decreased their affinity, as seen by a shift in their elution profile, when a gradient elution with mannose 6-phosphate
was employed. These results suggested that an ‘uncovered’ phosphate on the carbohydrate moiety of the enzymes was not essential
for binding but can enhance the binding affinity. |
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Keywords: | Lysosomal enzyme binding protein brain immobilisation binding requirements |
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