In:
Annals of the New York Academy of Sciences, Wiley, Vol. 986, No. 1 ( 2003-04), p. 150-154
Abstract:
A bstract : Steady‐state and pre‐steady‐state currents of Asn 776 mutants of Na,K‐ATPase are presented. The stationary current generated by N776Q strongly depends on the membrane potential, but has a negative slope, opposite to that of the wild‐type enzyme. The apparent rate constant of the reaction sequence E 1 P(Na + ) ↔ E 2 P + Na + of this mutant is rather independent of the membrane potential and is at resting and depolarizing membrane potential higher than that of the wild‐type enzyme. Thus, the voltage‐dependent increase of the rate coefficient of the wild type that is associated with extracellular Na + rebinding is almost absent in the N776Q mutant. These findings indicate that dislocating the carboxamide group of Asn 776 decreases the affinity of sodium at its extracellular binding site.
Type of Medium:
Online Resource
ISSN:
0077-8923
,
1749-6632
DOI:
10.1111/nyas.2003.986.issue-1
DOI:
10.1111/j.1749-6632.2003.tb07152.x
Language:
English
Publisher:
Wiley
Publication Date:
2003
detail.hit.zdb_id:
2834079-6
detail.hit.zdb_id:
211003-9
detail.hit.zdb_id:
2071584-5
SSG:
11