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Structure and expression of subunit A from the bovine chromaffin cell vacuolar ATPase
Author(s) -
Pan Ying-Xian,
Xu Jin,
Strasser Jane E.,
Howell Michael,
Dean Gary E.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81158-5
Subject(s) - protein subunit , complementary dna , microbiology and biotechnology , biology , biochemistry , peptide sequence , protein primary structure , fusion protein , atpase , antiserum , enzyme , recombinant dna , gene , antibody , immunology
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.