8-N-3-3 `-biotnyl-ATP, a novel monofunctional reagent: Differences in the F-1- and V-1-ATPases by means of the ATP analogue
DC Element | Wert | Sprache |
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dc.contributor.author | Schafer, HJ | |
dc.contributor.author | Coskun, U | |
dc.contributor.author | Eger, O | |
dc.contributor.author | Godovac-Zimmermann, J | |
dc.contributor.author | Wieczorek, H | |
dc.contributor.author | Kagawa, Y | |
dc.contributor.author | Gruber, G | |
dc.date.accessioned | 2021-12-23T16:21:53Z | - |
dc.date.available | 2021-12-23T16:21:53Z | - |
dc.date.issued | 2001 | |
dc.identifier.issn | 0006291X | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/14064 | - |
dc.description.abstract | A novel photoaffinity label, 8-N-3-3'-biotinyl-ATP, has been synthesized. The introduction of an additional biotin residue is advantageous for easy detection of labeled proteins. This could be first tested by reaction with the F-1-ATPase from the thermophilic bacterium PS3 (TF1). UV irradiation of TF1 in the presence of 8-N-3-3'-biotinyl-ATP results in a nucleotide-dependent binding of the analogue in the noncatalytic a and the catalytic beta subunits of TF1, demonstrating the suitability of this analogue as a potential photoaffinity label. Reaction with the V-1-ATPase, however, led to labeling of subunit E, which has been suggested as a structural and functional homologue of the gamma subunit of the F-ATPases. MALDI-TOF mass spectrometry has been used to map the regions of subunit E involved in the binding of 8-N-3-3'-biotiinyl-ATP. (C) 2001 Academic Press. | |
dc.language.iso | en | |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | |
dc.relation.ispartof | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | |
dc.subject | 5'-TRIPHOSPHATE | |
dc.subject | 8-AZIDO-ATP | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | Biophysics | |
dc.subject | COATED VESICLE | |
dc.subject | F-1-ATPase | |
dc.subject | GAMMA-SUBUNIT | |
dc.subject | H+-translocating vacuolar-type ATPase | |
dc.subject | HEART MITOCHONDRIAL ATPASE | |
dc.subject | Manduca sexta | |
dc.subject | NUCLEOTIDE-BINDING-SITES | |
dc.subject | PHOTOAFFINITY LABEL | |
dc.subject | photoaffinity labeling | |
dc.subject | RESOLUTION | |
dc.subject | thermophilic bacterium PS3 | |
dc.subject | V-1-ATPase | |
dc.subject | V-ATPASE | |
dc.subject | VACUOLAR (H+)-ATPASE | |
dc.title | 8-N-3-3 `-biotnyl-ATP, a novel monofunctional reagent: Differences in the F-1- and V-1-ATPases by means of the ATP analogue | |
dc.type | journal article | |
dc.identifier.doi | 10.1006/bbrc.2001.5502 | |
dc.identifier.isi | ISI:000170966200057 | |
dc.description.volume | 286 | |
dc.description.issue | 5 | |
dc.description.startpage | 1218 | |
dc.description.endpage | 1227 | |
dc.contributor.orcid | 0000-0003-4375-3144 | |
dc.contributor.researcherid | F-4683-2011 | |
dc.contributor.researcherid | E-6863-2010 | |
dc.identifier.eissn | 10902104 | |
dc.publisher.place | 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA | |
dcterms.isPartOf.abbreviation | Biochem. Biophys. Res. Commun. | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | WiHe990 | - |
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geprüft am 18.05.2024