Expression, Purification, and Binding Properties of Human Cellular Retinoic Acid-Binding Protein Type I and Type II
dc.contributor.author | Fogh K. , | en_US |
dc.contributor.author | Voorhees J. J. , | en_US |
dc.contributor.author | Astrom A. , | en_US |
dc.date.accessioned | 2006-04-10T15:54:43Z | |
dc.date.available | 2006-04-10T15:54:43Z | |
dc.date.issued | 1993-02-01 | en_US |
dc.identifier.citation | Fogh K., , Voorhees J. J., , Astrom A., (1993/02/01)."Expression, Purification, and Binding Properties of Human Cellular Retinoic Acid-Binding Protein Type I and Type II." Archives of Biochemistry and Biophysics 300(2): 751-755. <http://hdl.handle.net/2027.42/31000> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B6WB5-45PTR1M-F6/2/bdfa66bd9a35415d79c36dfa0c0dcb74 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/31000 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=8382035&dopt=citation | en_US |
dc.description.abstract | Human cellular retinoic acid-binding protein (CRABP) type I and type II were expressed in Escherichia coli from cloned cDNAs. Expressed proteins were purified by gel filtration and ion-exchange chromatography, resulting in highly pure proteins. The yield after gel filtration was approximately 50 mg/liter bacterial culture. In binding studies the equilibrium dissociation constant, Kd, of retinoic acid (RA) for E. coli-derived CRABP-I and CRABP-II was 6.8 and 39 nM, respectively. The Kd of the synthetic retinoid analog CD 367 was 2.2 nM for CRABP-I and 3.0 nM for CRABP-II. RA competed with the binding of CD 367 to CRABP-I and CRABP-II with IC50 values of 20.0 and 90.0 nM, respectively. Retinoid analogs competed with the binding of CD 367 to CRABP-I and CRABP-II in the following order: (p-[(E)-2-(5,6,7,8-tetrahydro-5,5,8,8-tetramethyl-2-naphtyl)-1-propenyl]benzoic acid (TTNPB) > 4-oxo-RA > 4-OH-RA > 13-cis-RA = 9-cis-RA. m-carboxy-TTNPB and CD 271 were found not to compete with the binding of CD 367 to CRABP-I or CRABP-II even at 500-fold molar excess. These data demonstrate that E. coli-derived CRABP-I has a higher affinity for RA than CRABP-II and that retinoic acid metabolites have a lower affinity for these proteins. The observed difference in affinity for RA supports the idea that CRARP-I, which is constitutively expressed, and CRABP-II, which is induced by RA, have different functions in the cell. In addition, 9-cis-RA, a natural ligand for the retinoid X receptors, is not a physiological ligand for either CRABP-I or CRABP-II. | en_US |
dc.format.extent | 410564 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 | Expression, Purification, and Binding Properties of Human Cellular Retinoic Acid-Binding Protein Type I and Type II | 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 Dermatology, University of Michigan, Kresge 1 R6558, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationum | Department of Dermatology, University of Michigan, Kresge 1 R6558, Ann Arbor, MI 48109, USA | en_US |
dc.contributor.affiliationum | Department of Dermatology, University of Michigan, Kresge 1 R6558, Ann Arbor, MI 48109, USA | en_US |
dc.identifier.pmid | 8382035 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/31000/1/0000675.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1006/abbi.1993.1104 | 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.