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Adenosine and hypoxanthine transport in horse erythrocytes: evidence for a polymorphism in the transport of hypoxanthine via a sodium‐dependent cotransporter

Jarvis, Simon M., Harris, R.C. (1998) Adenosine and hypoxanthine transport in horse erythrocytes: evidence for a polymorphism in the transport of hypoxanthine via a sodium‐dependent cotransporter. Journal of Physiology, 83 (2). pp. 203-209. ISSN 0022-3751. (doi:10.1113/expphysiol.1998.sp004104) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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http://dx.doi.org/10.1113/expphysiol.1998.sp004104

Abstract

The inward transport of two purines, adenosine and hypoxanthine, at 37 degrees C by horse erythrocytes was compared. No mediated transport of adenosine was detected in horse erythrocytes, nor was saturable, high‐affinity binding of the potent facilitated‐diffusion inhibitor nitrobenzylthioinosine demonstrable in horse erythrocyte membranes. In contrast, erythrocytes from most horses possessed a saturable sodium‐dependent hypoxanthine transporter (apparent K(m), 100 +/− 28 microM; Vmax, 0.20 +/− 0.08 mmol (l cells)‐1 h‐1; means +/− S.E.M., n = 5). Guanine inhibited hypoxanthine influx (apparent Ki, 24 +/− 6 microM), but adenine and xanthine had no effect. Unlike human erythrocytes, no sodium‐independent hypoxanthine transporter was detected in horse erythrocytes. There are, however, a small number of animals (approximately 15%) whose erythrocytes fail to transport hypoxanthine. This variation appears to be under genetic control, but the precise nature of the control is unknown.

Item Type: Article
DOI/Identification number: 10.1113/expphysiol.1998.sp004104
Additional information: Volume: 499P Special Issue: Sp. Iss. SI Pages: P50-P50 Published: FEB 1997
Subjects: Q Science
Q Science > QP Physiology (Living systems)
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: M.A. Ziai
Date Deposited: 21 Sep 2009 10:47 UTC
Last Modified: 10 Jun 2019 15:09 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/18126 (The current URI for this page, for reference purposes)
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