Abstract
A1 adenosine receptors from different tissues and species were photoaffinity
labelled and then the carbohydrate content was examined by both enzymatic
and chemical treatment. Sodium dodecyl sulfate-polyacrylamide gel
electrophoresis of the labelled membrane receptors shows that neuraminidase
treatment alters the electrophoretic mobility of the receptor band
indicating the presence of terminal neuraminic acids. Neuraminidase
digestion does not influence the binding characteristics of the receptor.
The totally deglycosylated receptor protein obtained by chemical
treatment has an apparent molecular weight of 32,000.
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