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

Jarvis, Simon M. and Harris, Roger C. (1998) Adenosine and hypoxanthine transport in horse erythrocytes: Evidence for a polymorphism in the transport of hypoxanthine via a sodium-dependent cotransporter. In: Experimental Physiology. Cambridge Univ Press pp. 203-209. (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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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 mu M; V-max, 0.20 +/- 0.08 mmol (1 cells)(-1) h(-1); means +/- S.E.M., n = 5). Guanine inhibited hypoxanthine influx (apparent K-i, 24 +/- 6 mu M), 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 (similar to 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: Conference or workshop item (Paper)
Additional information: Conference Information: Meeting of the Physiological-Society in Honor of Wilfred F Widdas SHEFFIELD, ENGLAND, JAN 05, 1997 Physiol Soc Document Type: Proceedings Paper
Subjects: Q Science
Q Science > QP Physiology (Living systems)
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: M.A. Ziai
Date Deposited: 05 Apr 2009 07:55
Last Modified: 23 Apr 2014 15:28
Resource URI: https://kar.kent.ac.uk/id/eprint/17380 (The current URI for this page, for reference purposes)
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