Studies on Herbicide Binding in Photosystem II Membrane Fragments from Spinach

dc.contributor.authorFromme, R.
dc.contributor.authorRenger, G.
dc.date.accessioned2018-11-10T16:39:00Z
dc.date.available2018-11-10T16:39:00Z
dc.date.issued1990
dc.description.abstractThe mechanism of atrazine binding and its modification by Chelex-100-induced Ca2+ depletion and proteolytic degradation by trypsin, was analyzed in PS II membrane fragments from spinach. It was found: 1) Chelex-100 treatment leads in a comparatively slow process (t1/2 = 5 - 10 min) to Ca2+ re moval from a site that is characterized by a high affinity as reflected by KD values of the order of 10-7M. The number of these binding sites was found to be almost one per PS II in samples washed twice with Ca2+ -free buffer. 2) Chelex-100 treatment does not affect the affinity of atrazine binding but increases the susceptibility to proteolytic attack by trypsin. 3) The electron transport activity is only slightly affected by Chelex-100 treatment. 4) The atrazine binding exhibits a rather small T-dependence within the physiological range of 7 °C to 27 °C. The implications of these findings for herbicide binding are discussed.en
dc.identifier.eissn1865-7125
dc.identifier.issn0939-5075
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/8501
dc.identifier.urihttp://dx.doi.org/10.14279/depositonce-7647
dc.language.isoen
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/3.0/
dc.subject.ddc570 Biowissenschaften; Biologiede
dc.subject.otheratrazine bindingen
dc.subject.otherPhotosystem IIen
dc.subject.otherCa2+ effectsen
dc.subject.othertemperature dependenceen
dc.subject.othermild proteolysisen
dc.titleStudies on Herbicide Binding in Photosystem II Membrane Fragments from Spinachen
dc.typeArticleen
dc.type.versionpublishedVersionen
dcterms.bibliographicCitation.doi10.1515/znc-1990-0511
dcterms.bibliographicCitation.issue5
dcterms.bibliographicCitation.journaltitleZeitschrift für Naturforschung Cde
dcterms.bibliographicCitation.originalpublishernameDe Gruyteren
dcterms.bibliographicCitation.originalpublisherplaceBerlinen
dcterms.bibliographicCitation.pageend378
dcterms.bibliographicCitation.pagestart373
dcterms.bibliographicCitation.volume45
tub.accessrights.dnbfree
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemiede
tub.affiliation.facultyFak. 2 Mathematik und Naturwissenschaftende
tub.affiliation.instituteInst. Chemiede
tub.publisher.universityorinstitutionTechnische Universität Berlinde

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