Structure and expression of subunit A from the bovine chromaffin cell vacuolar ATPase

Ying Xian Pan, Jin Xu, Jane E. Strasser, Michael Howell, Gary E. Dean

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

Subunit A of the vacuolar H+-ATPase class is thought to be responsible for the ATP hydrolysis which drives proton-pumping. We report here the cloning and sequence determination of the first mammalian cDNA encoding a bovine vacuolar ATPase subunit A from an adrenal medulla cDNA library. Northern blots of bovine adrenal medulla RNA reveal a message of approximately 3.8 kb. The predicted peptide sequence, consisting of 618 amino acids with a calculated molecular weight of 68397 daltons, is similar to the sequences of the three known subunit A proteins. β-Galactosidase-subunit A fusion proteins were immuno-decorated by an antiserum raised to the subunit A protein from corn coleoptile vacuoles.

Original languageEnglish (US)
Pages (from-to)89-92
Number of pages4
JournalFEBS Letters
Volume293
Issue number1-2
DOIs
StatePublished - Nov 1991
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Genetics
  • Molecular Biology
  • Biophysics
  • Structural Biology
  • Biochemistry
  • Cell Biology

Keywords

  • Bovine adrenal medulla
  • H-ATPase
  • cDNA cloning: Subunit structure

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