Human adenosine deaminase : Stoichiometry of the adenosine deaminase-binding protein complex
dc.contributor.author | Daddona, Peter E. | en_US |
dc.contributor.author | Kelley, William N. | en_US |
dc.date.accessioned | 2006-04-07T17:31:53Z | |
dc.date.available | 2006-04-07T17:31:53Z | |
dc.date.issued | 1979-10-24 | en_US |
dc.identifier.citation | Daddona, Peter E., Kelley, William N. (1979/10/24)."Human adenosine deaminase : Stoichiometry of the adenosine deaminase-binding protein complex." Biochimica et Biophysica Acta (BBA) - Protein Structure 580(2): 302-311. <http://hdl.handle.net/2027.42/23469> | en_US |
dc.identifier.uri | http://www.sciencedirect.com/science/article/B73GJ-47S1446-83/2/af034399cc16ea9960b05513b06e5ab1 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/23469 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=518903&dopt=citation | en_US |
dc.description.abstract | In many human tissues adenosine deaminase exists as a large molecular weight complex (large form) composed of adenosine deaminase and an adenosine deaminase binding protein. The molar ratio of adenosine deaminase to binding protein in this large form complex appears to be 2 : 1, respectively, based on several observations. Scatchard-type analysis of the binding of 125I-labeled adenosine deaminase to purified binding protein indicates that 2.15 mol of adenosine deaminase are bound to 1 mol of binding protein. Chemical cross-linking of 125I-labeled adenosine deaminase-binding protein complex (large form) with glutaraldehyde produces 6 cross-linked species with molecular weights consistent with the proposed 2 to 1 stoichiometry. Sedimentation equilibrium analyses reveal a native molecular weight of 300 890 for the adenosine deaminase-binding protein complex (large form), 37 500 for small form adenosine deaminase, and 213 300 for the binding protein. A 2 : 1 molar ratio of adenosine deaminase and binding protein in the large form complex is most consistent with these molecular weight estimates. | en_US |
dc.format.extent | 642130 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 | Human adenosine deaminase : Stoichiometry of the adenosine deaminase-binding protein complex | 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 | Departments of Internal Medicine and Biological Chemistry, Human Purine Research Center, University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.contributor.affiliationum | Departments of Internal Medicine and Biological Chemistry, Human Purine Research Center, University of Michigan Medical School, Ann Arbor, MI 48109, U.S.A. | en_US |
dc.identifier.pmid | 518903 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/23469/1/0000422.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1016/0005-2795(79)90143-0 | en_US |
dc.identifier.source | Biochimica et Biophysica Acta | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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