A Comparative Study of Human Muscle and Brain Creatine Kinases Expressed in Escherichia coli
dc.contributor.author | Kenyon, George L. | en_US |
dc.contributor.author | Babbitt, Patricia C. | en_US |
dc.contributor.author | McLeish, Michael J. | en_US |
dc.contributor.author | Chen, Lorenzo H. | en_US |
dc.contributor.author | White, Camille B. | en_US |
dc.date.accessioned | 2006-09-11T15:39:23Z | |
dc.date.available | 2006-09-11T15:39:23Z | |
dc.date.issued | 2000-01 | en_US |
dc.identifier.citation | Chen, Lorenzo H.; White, Camille B.; Babbitt, Patricia C.; McLeish, Michael J.; Kenyon, George L.; (2000). "A Comparative Study of Human Muscle and Brain Creatine Kinases Expressed in Escherichia coli." Journal of Protein Chemistry 19(1): 59-66. <http://hdl.handle.net/2027.42/45086> | en_US |
dc.identifier.issn | 0277-8033 | en_US |
dc.identifier.issn | 1573-4943 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/45086 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=10882173&dopt=citation | en_US |
dc.description.abstract | We report the expression of the human muscle (CK-MM) and brain (CK-BB) creatine kinases in Escherichia coli . The proteins have been purified to apparent homogeneity and several of their physical and kinetic properties investigated. In the process, we have conclusively verified the correct DNA sequence of the genes encoding the respective isozymes, and determined the correct primary structure and mass of the gene products. Alignment of the primary sequences of these two enzymes shows 81% sequence identity with each other, and no obvious gross structural differences. However, Western blot analyses demonstrated the general lack of antigenic cross-reactivity between these isozymes. Preliminary kinetic analyses show the K m and k cat values for the creatine and MgATP substrates are similar to values reported for other isozymes from various tissues and organisms. The human muscle and brain CKs do not, however, exhibit the synergism of substrate binding that is observed, for example, in rabbit muscle creatine kinase. | en_US |
dc.format.extent | 79337 bytes | |
dc.format.extent | 3115 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.language.iso | en_US | |
dc.publisher | Kluwer Academic Publishers-Plenum Publishers; Plenum Publishing Corporation ; Springer Science+Business Media | en_US |
dc.subject.other | Brain | en_US |
dc.subject.other | Purification | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | Animal Anatomy / Morphology / Histology | en_US |
dc.subject.other | Organic Chemistry | en_US |
dc.subject.other | Bioorganic Chemistry | en_US |
dc.subject.other | Biochemistry, General | en_US |
dc.subject.other | Creatine Kinase | en_US |
dc.subject.other | Human | en_US |
dc.subject.other | Expression | en_US |
dc.subject.other | Muscle | en_US |
dc.subject.other | Kinetics | en_US |
dc.title | A Comparative Study of Human Muscle and Brain Creatine Kinases Expressed in Escherichia coli | en_US |
dc.type | Article | en_US |
dc.subject.hlbsecondlevel | Natural Resources and Environment | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbsecondlevel | Ecology and Evolutionary Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, 94143; Division of Medicinal Chemistry, University of Michigan, Ann Arbor, Michigan, 48109 | en_US |
dc.contributor.affiliationum | Division of Medicinal Chemistry, University of Michigan, Ann Arbor, Michigan, 48109 | en_US |
dc.contributor.affiliationother | Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, 94143 | en_US |
dc.contributor.affiliationother | Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, 94143 | en_US |
dc.contributor.affiliationother | Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, California, 94143 | en_US |
dc.contributor.affiliationumcampus | Ann Arbor | en_US |
dc.identifier.pmid | 10882173 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/45086/1/10930_2004_Article_225277.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1023/A:1007047026691 | en_US |
dc.identifier.source | Journal of Protein Chemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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