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Membrane proteins and urea and acetamide transport in the human erythrocyte

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Summary

Previous studies have shown that urea and acetamide traverse the erythrocyte membrane by way of facilitated diffusion. The nature of this selective pathway is unknown. The present studies investigate the effects of proteolytic enzymes and crosslinking agents on amide transport. Cleavage of the erythrocyte membrane surface by pronase or trypsin had no effect on urea and acetamide permeability or inhibition by phloretin. These findings suggest that the sialoglycopeptide segment of the sialoglycoproteins is not critical to urea and acetamide transport. In addition, extensive crosslinking of membrane proteins with glutaraldehyde had no effect on amide transport in the absence or presence of phloretin.

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Authors and Affiliations

  1. Department of Medicine, Department of Biochemistry and Unit for Research in Heart, Lung, and Ageing, Albert Einstein College of Medicine, 10461, New York, N.Y.

    Michael A. Kaplan M.D., Richard M. Hays & Olga O. Blumenfeld

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  1. Michael A. Kaplan M.D.
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  2. Richard M. Hays
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  3. Olga O. Blumenfeld
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Kaplan, M.A., Hays, R.M. & Blumenfeld, O.O. Membrane proteins and urea and acetamide transport in the human erythrocyte. J. Membrain Biol. 20, 181–190 (1975). https://doi.org/10.1007/BF01870635

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  • DOI: https://doi.org/10.1007/BF01870635

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