Soluble cytochrome b5 from human erythrocytes
dc.contributor.author | Passon, P. G. | en_US |
dc.contributor.author | Reed, D. W. | en_US |
dc.contributor.author | Hultquist, Donald E. | en_US |
dc.date.accessioned | 2006-04-17T16:47:54Z | |
dc.date.available | 2006-04-17T16:47:54Z | |
dc.date.issued | 1972-07-12 | en_US |
dc.identifier.citation | Passon, P. G., Reed, D. W., Hultquist, D. E. (1972/07/12)."Soluble cytochrome b5 from human erythrocytes." Biochimica et Biophysica Acta (BBA) - Bioenergetics 275(1): 51-61. <http://hdl.handle.net/2027.42/34069> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6T1S-47PP0F8-25/2/5d533daf31f0b6d9fd3c6bc6e5a650ea | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/34069 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=4340269&dopt=citation | en_US |
dc.description.abstract | 1. A hemeprotein with properties similar to microsomal cytochrome b5 has been detected in the supernatant fraction of hemolysates of human, beef, and rabbit erythrocytes. A method has been developed for determining the amount of this soluble cytochrome in small volumes of blood. The amount of the protein decreases during cell storage at 4 [deg]C. Blood cells rich in reticulocytes contain more of the protein than do mature cells.2. The cytochrome has been purified from human erythrocytes by a procedure which employs chromatography on Amberlite CG-50 and DETE-cellulose, ultrafiltration, and gel filtration. The purified protein sedimented in the ultracentrifuge as a single peak with an s20, w of 1.40. However, minor impurities were detected by polyacrylamide disc electrophoresis.3. The molecular weight of the purified protein has been calculated to be 14600 from sedimentation and diffusion measurements and 18400 as determined by gel filtration. The prosthetic group has been identified as protoheme IX. The spectral properties of the hemeprotein are those of a low spin heme complex. The EPR spectrum of the oxidized form shows g values of 3.03, 2.21, and 1.39 and the visible spectrum has a Soret absorbance maximum at 413 nm. The protein is reducible by dithionite or NADH plus cytochrome b5 reductase and the reduced form shows absorbance maxima at 423, 527, and 556 nm with a shoulder at 560 nm.4. The cytochrome b5 differs from the other B-type cytochrome of erythrocyte, S-protein (hemeprotein 559), and is not derived from this protein. The erythrocyte cytochrome b5 is similar to the cytochrome b5 solubilized from liver microsomes in terms of spectral properties, molecular weight, prosthetic group, and reactivity. | en_US |
dc.format.extent | 707665 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 | Soluble cytochrome b5 from human erythrocytes | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48 104, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48 104, U.S.A. | en_US |
dc.contributor.affiliationum | Department of Biological Chemistry, University of Michigan, Ann Arbor, Mich. 48 104, U.S.A. | en_US |
dc.identifier.pmid | 4340269 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/34069/1/0000347.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2728(72)90023-0 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | 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.