Ref cell hydrolases: Glycosidase activities in human erythrocyte plasma membranes |
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Authors: | H. Bruce Bosmann |
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Affiliation: | (1) Department of Pharmacology and Toxicology, University of Rochester, School of Medicine and Dentistry, 14620 Rochester, New York |
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Abstract: | Summary Human erythrocyte plasma membranes were found to contain the following glycosidases: α- and β-glucosidase, α- and β-galactosidase, α- and β-fucosidase, β-N-acetylglucosaminidase, β-N-acetylgalactosaminidase, β-xylosidase and α-mannosidase. All the enzymes except β-fucosidase had activity interpreted to be on the external surface of the plasma membrane. The enzymes had optimum pH values of 5.2 to 5.0 and temperatures of 37 to 40°C. The enzymes were not greatly activated by divalent cations but Hg++ and Pb++ were inhibitory. The enzyme extract of the human erythrocyte plasma membranes liberated carbohydrate from intact red cells, which lead to the speculation that the glycosidases might function to modify the erythrocyte plasma membrane. The author is a Research Career Development Awardee of the National Institute of General Medical Sciences. |
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