caa a22 4500 475743873 CHVBK 20180406123507.0 cr unu---uuuuu 170329e20000101xx s 000 0 eng 10.1023/A:1007047026691 doi (NATIONALLICENCE)springer-10.1023/A:1007047026691 A Comparative Study of Human Muscle and Brain Creatine Kinases Expressed in Escherichia coli [Elektronische Daten] [Lorenzo Chen, Camille White, Patricia Babbitt, Michael McLeish, George Kenyon] 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. Plenum Publishing Corporation, 2000 Creatine kinase nationallicence human nationallicence expression nationallicence brain nationallicence muscle nationallicence purification nationallicence kinetics nationallicence Chen Lorenzo Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, San Francisco, California aut White Camille Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, San Francisco, California aut Babbitt Patricia Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, San Francisco, California aut McLeish Michael Division of Medicinal Chemistry, University of Michigan, 48109, Ann Arbor, Michigan aut Kenyon George Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, San Francisco, California aut Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/1(2000-01-01), 59-66 0277-8033 19:1<59 2000 19 10930 https://doi.org/10.1023/A:1007047026691 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1007047026691 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Chen Lorenzo Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, San Francisco, California aut NATIONALLICENCE 700 1- White Camille Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, San Francisco, California aut NATIONALLICENCE 700 1- Babbitt Patricia Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, San Francisco, California aut NATIONALLICENCE 700 1- McLeish Michael Division of Medicinal Chemistry, University of Michigan, 48109, Ann Arbor, Michigan aut NATIONALLICENCE 700 1- Kenyon George Department of Pharmaceutical Chemistry, University of California, San Francisco, 94143, San Francisco, California aut NATIONALLICENCE 773 0- Journal of Protein Chemistry Kluwer Academic Publishers-Plenum Publishers 19/1(2000-01-01), 59-66 0277-8033 19:1<59 2000 19 10930 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer