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Quantitative affinity chromatographic studies of mitochondrial cytochrome c binding to bacterial photosynthetic reaction center, reconstituted in liposome membranes and immobilized by detergent dialysis and avidin-biotin binding
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Chemistry, Department of Biochemistry.
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2000 (English)In: ANALYTICAL BIOCHEMISTRY, ISSN 0003-2697, Vol. 280, no 1, 94-102 p.Article in journal (Refereed) Published
Abstract [en]

In order to study the affinity binding of c-type cytochromes to the photosynthetic reaction center (RC) by quantitative affinity chromatography (QAC), RC from Rhodobacter sphaeroides was reconstituted into liposomes composed of egg phosphatidylcholine (EP

Place, publisher, year, edition, pages
ACADEMIC PRESS INC , 2000. Vol. 280, no 1, 94-102 p.
Keyword [en]
RHODOPSEUDOMONAS-SPHAEROIDES R-26; GLUCOSE-TRANSPORTER GLUT1; PROTEIN-LIPID VESICLES; ELECTRON-TRANSFER; CYTOCHALASIN-B; GEL BEADS; PROTEOLIPOSOMES; BILAYERS; DYNAMICS; PHASE
Identifiers
URN: urn:nbn:se:uu:diva-38007OAI: oai:DiVA.org:uu-38007DiVA: diva2:65906
Note
Addresses: Miyake J, Natl Inst Adv Interdisciplinary Res, 1-1-4 Higashi, Tsukuba, Ibaraki 3058562, Japan. Natl Inst Adv Interdisciplinary Res, Tsukuba, Ibaraki 3058562, Japan. Natl Inst Biosci & Human Technol, Tsukuba, Ibaraki 3058566, Japan. Univ UppsalaAvailable from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-14

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