Hydrodynamic Properties of the Chromaffin Granule Hydrogen Ion Pumping Adenosinetriphosphatase

Gary E. Dean, Gary Rudnic, William Agnew, Pamlea J. Nelson

Research output: Contribution to journalArticlepeer-review

Abstract

We have determined the hydrodynamic properties of detergent-solubilized ATPase, which is coupled to H+ pumping in bovine adrenal chromaffin granules, by sedimentation equilibrium centrifugation and gel permeation chromatography. The protein solubilized with detergent containing phosphatidylserine sediments as a particle of 264000 daltons and partial specific volume 0.829 cm3/g. Assuming a protein v of 0.73 and using the v measured for detergent and lipid mixed micelles of 0.93 cm3/g, we calculated that the protein component has a mass of 134000 daltons and that the equivalent of approximately 1.5 micelles of detergent are bound per particle. The particle exhibits a Stokes radius of 43 A, which, together with the calculated particle volume, indicates an axial ratio close to 1. We conclude that the ATPase is an intrinsic membrane protein with a structure very different from that of mitochondrial F1Fo ATPase.

Original languageEnglish (US)
Pages (from-to)2301-2305
Number of pages5
JournalBiochemistry
Volume26
Issue number8
DOIs
StatePublished - 1987

ASJC Scopus subject areas

  • Biochemistry

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