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

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.

journal_name

Exp Physiol

journal_title

Experimental physiology

authors

Jarvis SM,Harris RC

doi

10.1113/expphysiol.1998.sp004104

subject

Has Abstract

pub_date

1998-03-01 00:00:00

pages

203-9

issue

2

eissn

0958-0670

issn

1469-445X

journal_volume

83

pub_type

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