Properties of spinach ferredoxin in anaerobic urea solution: A comparison with the native protein
dc.contributor.author | Petering, David H. | en_US |
dc.contributor.author | Palmer, Graham | en_US |
dc.date.accessioned | 2006-04-17T15:05:46Z | |
dc.date.available | 2006-04-17T15:05:46Z | |
dc.date.issued | 1970-12 | en_US |
dc.identifier.citation | Petering, David H., Palmer, Graham (1970/12)."Properties of spinach ferredoxin in anaerobic urea solution: A comparison with the native protein." Archives of Biochemistry and Biophysics 141(2): 456-464. <http://hdl.handle.net/2027.42/32649> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-4DW2N34-2H5/2/60a7528622c64a39ac2404991fbc78f1 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/32649 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4322287&dopt=citation | en_US |
dc.description.abstract | The preparation of spinach ferredoxin by a modification of the method of Keresztes-Nagy and Margoliash which is particularly convenient for large-scale operation is described.The optical, CD, and EPR spectra of this protein are studied in 5 urea as a function of ionic strength. At high ionic strength the various spectra are very similar to the native protein; at low ionic strength all three spectral parameters are greatly changed.The reactivity of the protein with mercurial and iodoacetamide is compared. The very high reactivity of the former is rationalized by assuming an initial reaction with the sulfide moieties. Iodoacetamide reacts only with accompanying denaturation by an all-or-none mechanism. At most only one sulfhydryl is available for reaction, even in 5 urea. This is consistent with the assumption that the mercaptides function as metal ligands.A very sensitive instrument for the amperometric titration of SH groups is described. | en_US |
dc.format.extent | 876122 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Elsevier | en_US |
dc.title | Properties of spinach ferredoxin in anaerobic urea solution: A comparison with the native protein | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Public Health | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Michigan 48105, USA; NSF Predoctoral Fellow; Department of Chemistry, Northwestern University, Evanston, Illinois. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, Biophysics Research Division, Institute of Science and Technology, University of Michigan, Ann Arbor, Michigan 48105, USA; Career Development Awardee, GM-K3-21,213 | en_US |
dc.identifier.pmid | 4322287 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/32649/1/0000013.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0003-9861(70)90162-1 | en_US |
dc.identifier.source | Archives of Biochemistry and Biophysics | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.