DC Element | Wert | Sprache |
dc.contributor.author | Wieczorek, H | |
dc.contributor.author | Gruber, G | |
dc.contributor.author | Harvey, WR | |
dc.contributor.author | Huss, M | |
dc.contributor.author | Merzendorfer, H | |
dc.contributor.author | Zeiske, W | |
dc.date.accessioned | 2021-12-23T16:13:48Z | - |
dc.date.available | 2021-12-23T16:13:48Z | - |
dc.date.issued | 2000 | |
dc.identifier.issn | 00220949 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/10760 | - |
dc.description.abstract | H+ V-ATPases (V-ATPases) are found in two principal locations, in endomembranes and in plasma membranes. The plasma membrane V-ATPase from the midgut of larval Manduca sexta is the sole energizer of all transepithelial secondary transport processes. At least two properties make the lepidopteran midgut a model tissue for studies of general aspects of V-ATPases. First, it is a rich source for purification of the enzyme and therefore for structural studies: 20 larvae provide up to 0.5 mg of holoenzyme, and soluble, cytosolic V-1 complexes can be obtained in even greater amounts off up to 2 mg, Second, midgut ion-tranport processes are strictly controlled by the regulation of the V-ATPase, which is the sole energizer of all ion transport in this epithelium. Recent advances in our understanding the structure of the V-1 and V-o complexes and of the regulation of the enzyme's biosynthesis and ion-transport activity will be discussed. | |
dc.description.sponsorship | NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASESUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [R01AI022444] Funding Source: NIH RePORTER; NIAID NIH HHSUnited States Department of Health & Human ServicesNational Institutes of Health (NIH) - USANIH National Institute of Allergy & Infectious Diseases (NIAID) [AI 22444] Funding Source: Medline | |
dc.language.iso | en | |
dc.publisher | COMPANY OF BIOLOGISTS LTD | |
dc.relation.ispartof | JOURNAL OF EXPERIMENTAL BIOLOGY | |
dc.subject | Biology | |
dc.subject | CRASSA VACUOLAR ATPASE | |
dc.subject | H+-translocating vacuolar-type ATPase | |
dc.subject | HORNWORM MANDUCA-SEXTA | |
dc.subject | Life Sciences & Biomedicine - Other Topics | |
dc.subject | MALPIGHIAN TUBULES | |
dc.subject | Manduca sexta | |
dc.subject | MESSENGER-RNA | |
dc.subject | midgut | |
dc.subject | MIDGUT EPITHELIUM | |
dc.subject | MITOCHONDRIA-RICH | |
dc.subject | PROTON PUMP | |
dc.subject | TOBACCO HORNWORM | |
dc.subject | TRANSCRIPTIONAL REGULATION | |
dc.subject | V-1 ATPase | |
dc.subject | V-1 complex | |
dc.subject | V-o complex | |
dc.subject | V-TYPE ATPASE | |
dc.title | Structure and regulation of insect plasma membrane H+V-ATPase | |
dc.type | journal article | |
dc.identifier.isi | ISI:000084963000015 | |
dc.description.volume | 203 | |
dc.description.issue | 1 | |
dc.description.startpage | 127 | |
dc.description.endpage | 135 | |
dc.publisher.place | BIDDER BUILDING CAMBRIDGE COMMERCIAL PARK COWLEY RD, CAMBRIDGE CB4 4DL, CAMBS, ENGLAND | |
dcterms.isPartOf.abbreviation | J. Exp. Biol. | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.dept | Universität Osnabrück | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | WiHe990 | - |
crisitem.author.netid | HuMa001 | - |
crisitem.author.netid | MeHa731 | - |