Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Z I Randhawa"'
Publikováno v:
Protein Science. 2:244-254
The folding pathway for a 150-amino acid recombinant form of the dimeric cytokine human macrophage colony-stimulating factor (M-CSF) has been studied. All 14 cysteine residues in the biologically active homodimer are involved in disulfide linkages. T
Autor:
W Newman, L D Beall, C W Carson, G G Hunder, N Graben, Z I Randhawa, T V Gopal, J Wiener-Kronish, M A Matthay
Publikováno v:
The Journal of Immunology. 150:644-654
A quantitative sandwich ELISA for E-selectin in the fluid phase (soluble E-selectin, sEs) has been developed that is sensitive to 100 pg/ml. The assay shows no reactivity with either L- or P-selectins. We have used this to determine the fate of E-sel
Publikováno v:
Journal of Biological Chemistry. 267:18488-18492
Thioesterase II is a 29-kDa monomer which, in certain specialized tissues, acts as a chain terminator in fatty acid synthesis by hydrolyzing medium-chain fatty acids from the fatty acid synthase. As with serine proteases, hydrolysis appears to involv
Autor:
Z I Randhawa, B N Green, L DeVeaux, John E. Cronan, H Cho, M L Narasimhan, Stuart Smith, J Naggert
Publikováno v:
Journal of Biological Chemistry. 266:11044-11050
The gene (tesB) encoding Escherichia coli thioesterase II, a low-abundance enzyme of unknown physiological function which can hydrolyze a broad range of acyl-CoA thioesters, has been localized by transposon mutagenesis, cloned and sequenced. A two-ci
Autor:
J. Cone, K Yamanishi, J. A. Wilkins, Z. I. Randhawa, P Hughes, Y Masui, H. E. Witkowska, P Arthur, S Yasuda, C Kletke
Publikováno v:
Biochemistry. 33(14)
Expression of the 17.5-kDa truncated form of human recombinant macrophage colony stimulating factor (rM-CSF, 4-153) in Escherichia coli is complicated by the replacement of methionine residues by norleucine. In order to detect and quantitate this mis
Publikováno v:
Protein science : a publication of the Protein Society. 2(2)
The folding pathway for a 150-amino acid recombinant form of the dimeric cytokine human macrophage colony-stimulating factor (M-CSF) has been studied. All 14 cysteine residues in the biologically active homodimer are involved in disulfide linkages. T
Autor:
W, Newman, L D, Beall, C W, Carson, G G, Hunder, N, Graben, Z I, Randhawa, T V, Gopal, J, Wiener-Kronish, M A, Matthay
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 150(2)
A quantitative sandwich ELISA for E-selectin in the fluid phase (soluble E-selectin, sEs) has been developed that is sensitive to 100 pg/ml. The assay shows no reactivity with either L- or P-selectins. We have used this to determine the fate of E-sel
Publikováno v:
The Journal of biological chemistry. 267(26)
Thioesterase II is a 29-kDa monomer which, in certain specialized tissues, acts as a chain terminator in fatty acid synthesis by hydrolyzing medium-chain fatty acids from the fatty acid synthase. As with serine proteases, hydrolysis appears to involv
Autor:
J, Naggert, M L, Narasimhan, L, DeVeaux, H, Cho, Z I, Randhawa, J E, Cronan, B N, Green, S, Smith
Publikováno v:
The Journal of biological chemistry. 266(17)
The gene (tesB) encoding Escherichia coli thioesterase II, a low-abundance enzyme of unknown physiological function which can hydrolyze a broad range of acyl-CoA thioesters, has been localized by transposon mutagenesis, cloned and sequenced. A two-ci
Publikováno v:
Methods in enzymology. 184