Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Kim Oikawa"'
Autor:
William A. Bridger, Leslie D. Hicks, William T. Wolodko, Edward R. Brownie, Michael N.G. James, Kim Oikawa, Cyril M. Kay, Jean-Christophe Rochet, Marie E. Fraser
Publikováno v:
Biochemistry. 39:11291-11302
Pig heart CoA transferase (EC 2.8.3.5) has been shown previously to adopt a homodimeric structure, in which each subunit has a molecular weight of 52 197 and consists of N- and C-domains linked by a hydrophilic linker or "hinge". Here we identify and
Autor:
Kim Oikawa, Hideaki Maekawa, Vasanthy Narayanaswami, Robert O. Ryan, Ryoichi Sato, Yoshio Yamauchi, Kozo Tsuchida, Cyril M. Kay, Paul M. M. Weers
Publikováno v:
European Journal of Biochemistry. 267:728-736
Apolipophorin III (apoLp-III) from the silkmoth, Bombyx mori, has been over-expressed in Escherichia coli, purified and characterized. Far-UV CD spectroscopic analysis revealed 65% alpha-helix secondary structure. Near-UV CD spectra obtained in buffe
Autor:
Kim Oikawa, Jean-Christophe Rochet, Leslie D. Hicks, Cyril M. Kay, William T. Wolodko, William A. Bridger
Publikováno v:
Biochemistry. 36:8807-8820
The enzyme CoA transferase from porcine heart (EC 2.8.3.5) is a homodimer; each subunit consists of two domains linked by a hydrophilic "hinge" region. We have prepared separate DNA segments encoding each of these domains. Incorporation of these two
Autor:
Vasanthy Narayanaswami, Kim Oikawa, Cyril M. Kay, Dean Schieve, Luis B. Agellon, Robert O. Ryan, M. Wientzek
Publikováno v:
Journal of Lipid Research, Vol 36, Iss 5, Pp 1066-1072 (1995)
To facilitate structure-function studies of Manduca sexta apolipophorin III (apoLp-III), its nucleotide coding sequence was cloned from a fat body cDNA library by in vitro DNA amplification. The amplification product was cloned in the pET expression
Publikováno v:
Archives of Insect Biochemistry and Physiology. 30:211-223
Chemical modification procedures were employed to neutralize charged amino acid side chains of apolipophorin III (apoLp-III). Glutamate plus aspartate carboxylate side chains were amidated while, in other experiments, the ϵ-amino groups of lysine re
Publikováno v:
Biochemistry. 33:3617-3624
Apolipophorin I11 (apoLp-111) from the migratory locust, Locusta migratoria, represents the only full-length apolipoprotein whose three-dimensional structure has been solved. In the present study, spectroscopic methods have been employed to investiga
Publikováno v:
Journal of Biological Chemistry. 269:4605-4612
Apolipophorin-III (apoLp-III), a hemolymph protein of Manduca sexta, can reversibly associate with the surface of lipoprotein particles. In order to examine the lipid-associated form of apoLp-III, the present studies investigate the structure and pro
Publikováno v:
Biochemistry. 32:6729-6736
A procedure for rapid isolation of lipid transfer protein (LTP) from commercially available rabbit plasma is described. Use of protease inhibitors was important for obtaining intact, stable LTP. After lipoproteins were precipitated from the plasma by
Publikováno v:
Journal of Biological Chemistry. 268:1525-1530
Apolipophorin III (apoLp-III) is a major protein in hemolymph of adult Manduca sexta. Although it normally exists in a lipid-free state, during sustained flight, apoLp-III functions as an apolipoprotein, reversibly associating with the surface of lip
Autor:
Kim Oikawa, Andre Herklotz, Thor J. Borgford, Fernando C. Reinach, Osnat Herzberg, Cyril M. Kay, Murali Chandra, Lawrence B. Smillie, John Moult, Joyce R. Pearlstone
Publikováno v:
Biochemistry. 31:6545-6553
A spectral probe mutant (F29W) of chicken skeletal muscle troponin C (TnC) has been prepared in which Phe-29 has been substituted by Trp. Residue 29 is at the COOH-terminal end of the A helix immediately adjacent to the Ca2+ binding loop of site I (r