The Journal of biological chemistry, 1998-05, Vol.273 (18), p.10939-10947
1998
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Details
- Autor(en) / Beteiligte
- Titel
- Identification and Characterization of a Novel 9.2-kDa Membrane Sector-associated Protein of Vacuolar Proton-ATPase from Chromaffin Granules
- Ist Teil von
- The Journal of biological chemistry, 1998-05, Vol.273 (18), p.10939-10947
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 1998
- Quelle
- MEDLINE
- Beschreibungen/Notizen
- Vacuolar proton-translocating ATPase (holoATPase and free membrane sector) was isolated from bovine chromaffin granules by blue native polyacrylamide gel electrophoresis. A 5-fold excess of membrane sector over holoenzyme was determined in isolated chromaffin granule membranes. M9.2, a novel extremely hydrophobic 9.2-kDa protein comprising 80 amino acids, was detected in the membrane sector. It shows sequence and structural similarity to Vma21p, a yeast protein required for assembly of vacuolar ATPase. A second membrane sector-associated protein (M8-9) was identified and characterized by amino-terminal protein sequencing.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0021-9258eISSN: 1083-351XDOI: 10.1074/jbc.273.18.10939Titel-ID: cdi_proquest_miscellaneous_79820751
- Format
- –
- Schlagworte
- ADENOSINETRIPHOSPHATASE, ADRENAL GLANDS, Amino Acid Sequence, AMINO ACID SEQUENCES, Animals, ATPASE, Base Sequence, BIOLOGICAL DIFFERENCES, BLUE NATIVE PAGE, CATTLE, CELL MEMBRANES, CHEMICAL COMPOSITION, Chromaffin Granules - enzymology, COMPLEMENTARY DNA, DNA, ELECTROPHORESIS, GENBANK/Y15285, GENBANK/Y15286, GENE EXPRESSION, Humans, HYDROLASES, MANKIND, Membrane Proteins - chemistry, Membrane Proteins - metabolism, MESSENGER RNA, Mice, MOLECULAR SEQUENCE DATA, NUCLEOTIDE SEQUENCE, PAGE, PDB/P81103, PDB/P81134, Proton-Translocating ATPases - metabolism, PURIFICATION, PYROPHOSPHATASES, Sequence Homology, Nucleic Acid, SPECIES DIFFERENCES, Vacuolar Proton-Translocating ATPases