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. 1986 Oct 1;239(1):77–81. doi: 10.1042/bj2390077

Proton-translocating adenosine triphosphatase of chromaffin-granule membranes. The active site is in the largest (70 kDa) subunit.

J M Percy, D K Apps
PMCID: PMC1147241  PMID: 2879537

Abstract

The proton-translocating adenosine triphosphatase (ATPase) of bovine chromaffin granules contains up to five different polypeptides. Its activity is inhibited by N-ethylmaleimide, and ATP protects the enzyme from inhibition. After treatment of membranes with N-[2-3H]ethylmaleimide, only one polypeptide is strongly radiolabelled: this is the largest (70 kDa) subunit of the proton-translocating ATPase. This subunit therefore contains the ATP-hydrolysing site. Two-dimensional electrophoresis reveals heterogeneity in this polypeptide.

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Selected References

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