Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Kurt Bill"'
Autor:
Dieter Zimmer, Natalie Lehmann, Olivier Heudi, Samuel Barteau, Olivier Kretz, Christian Bauer, Joerg Schmidt, Kurt Bill
Publikováno v:
Analytical Chemistry. 80:4200-4207
Although LC-MS methods are increasingly used for the absolute quantification of proteins, the lack of appropriate internal standard (IS) hinders the development of rapid and standardized analytical methods for both in vitro and in vivo studies. Here,
Autor:
Markus Heitzmann, Kurt Forrer, Thomas A. Millward, Peter Schumacher, Ulrich Längle, Kurt Bill
Publikováno v:
Biologicals : journal of the International Association of Biological Standardization. 36(1)
Previous studies on the effect of glycosylation on the elimination rate of antibodies have produced conflicting results. Here, we performed pharmacokinetic studies in mice with two preparations of a monoclonal IgG1 antibody enriched for complex type
Autor:
Kurt Bill, Angelo Azzi
Publikováno v:
Biochemical and Biophysical Research Communications. 120:124-130
Making use of a hetero-bifunctional reagent (succinimidyl 4-(p-maleimidophenyl)butyrate, SMPB), yeast cytochrome c was linked through a thioether bond to the maleimide group whereas the active N-hydroxysuccinimide ester site of the SMPB was used for
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 679:28-34
A method for simultaneous purification of cytochrome c reductase and cytochrome c oxidase using a cytochrome c affinity column is presented. Cytochrome c from Saccharomyces cerevisiae was linked to an activated thiol-Sepharose gel via its Cys-102 res
Publikováno v:
FEBS Letters. 120:248-250
Cytochrome c oxidase (EC 19.3 .l) is a membranebound enzyme which catalyses the reduction of molecular oxygen to water. The reducing equivalents for this reaction are provided by the natural substrate of the enzyme, ferrocytochrome c. Cytochromes c h
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 79(8)
An efficient affinity chromatography procedure for the isolation of mitochondrial cytochrome c oxidase and reductase is described. Saccharomyces cerevisiae cytochrome c was used as a ligand, bound to a thiol-Sepharose 4B gel through cysteine-107. In
Autor:
Kurt Bill, Angelo Azzi
Publikováno v:
Biochemical and biophysical research communications. 106(4)
A covalent chromatography technique is described for the preparation of an active cytochrome c oxidase from bovine heart devoid of subunit III. Yeast cytochrome c is immobilized on a Sepharose 4B gel, its cysteine 107 activated and reacted with the o
Publikováno v:
Methods in Enzymology ISBN: 9780121820268
Publisher Summary This chapter describes the affinity chromatography purification of cytochrome-c oxidase from bovine heart mitochondria and other sources. In the mitochondrial respiratory chain cytochrome- c oxidase catalyzes the electron transfer f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6168f3ba953aba1176a867516ee5ecb8
https://doi.org/10.1016/s0076-6879(86)26008-5
https://doi.org/10.1016/s0076-6879(86)26008-5
Publisher Summary This chapter focuses on the resolution of cytochrome- c oxidase. Cytochrome- c oxidase from bovine heart mitochondria is a multisubunit complex consisting of 13 polypeptides and four prosthetic groups, two hemes and two coppers. Hem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e5a3c3270f745089dfa9fc2706a261c4
https://doi.org/10.1016/s0076-6879(86)26009-7
https://doi.org/10.1016/s0076-6879(86)26009-7