Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Por-Hsiung Lai"'
Publikováno v:
Biochemical Journal. 394:249-257
Human serum contains factors that promote oxidative folding of disulphide proteins. We demonstrate this here using hirudin as a model. Hirudin is a leech-derived thrombin-specific inhibitor containing 65 amino acids and three disulphide bonds. Oxidat
Autor:
Langley, Keith E.1, Por-Hsiung Lai1, Wypych, Jette1, Everett, Richard R.1, Berg, Thor F.1, Krabill, L. F.2, Davis, Janice M.1, Souza, Lawrence M.1
Publikováno v:
European Journal of Biochemistry. 3/2/87, Vol. 163 Issue 2, p323-330. 8p. 2 Diagrams, 2 Charts, 7 Graphs.
Publikováno v:
Journal of Biological Chemistry. 276:4845-4852
The folding pathway of human epidermal growth factor (EGF) has been characterized by structural and kinetic analysis of the acid-trapped folding intermediates. Oxidative folding of the fully reduced EGF proceeds through 1-disulfide intermediates and
Publikováno v:
Protein Science. 8:1463-1468
Insulin-like growth factor (IGF-1) contains three disulfide bonds. In the presence of denaturant and thiol catalyst, IGF-1 shuffles its native disulfide bonds and denatures to form a mixture of scrambled isomers. The composition of scrambled IGF vari
Publikováno v:
The Journal of biological chemistry. 270(16)
Human epidermal growth factor (EGF) contains three disulfides and 53 amino acids. Reduced/denatured EGF refolds spontaneously in vitro to acquire its native structure. The mechanism of this folding process has been elucidated by structural analysis o
Publikováno v:
Journal of Biological Chemistry. 261:3116-3121
Erythropoietin is the primary regulator of red blood cell formation in mammals. Because of its extreme scarcity, very little information is available regarding structural features of this important glycoprotein. We report here the primary structure o
Autor:
Michael Benjamin Mann, Dennis Fenton, Larry B. Tsai, Michael L. Klein, Craig Curless, Por-Hsiung Lai, Bruce W. Altrock, Hsieng Sen Lu, William C. Kenney
Publikováno v:
Biochemical and Biophysical Research Communications. 156:733-739
Interleukin-2 produced from a recombinant E. coli was found to contain as much as 19% norleucine in place of methionine in a minimal medium fermentation. Medium supplementation experiments and use of a leucine-requiring mutant host strain indicated t
Publikováno v:
Archives of Biochemistry and Biophysics. 268:81-92
Molecular characteristics and secondary structures of recombinant methionyl human granulocyte colony stimulating factor produced by genetically engineered Escherichia coli are described. Limited radiolabeling of the protein with tritiated iodoacetate
Autor:
Por-hsiung Lai
Publikováno v:
Analytica Chimica Acta. 163:243-248
Improved techniques for preparing samples and sequencing reagents have been developed to achieve highly sensitive protein sequencing. These improvements include a new sequencing buffer system which gives extremely low chromatographic background, a me
Publikováno v:
Biochemical and Biophysical Research Communications. 136:679-684
Recombinant human interferon-γ was phosphorylated with ATP and c-AMP-dependent protein kinase. After phosphorylation, interferon-γ was separated from the adenosine phosphates and the kinase and analyzed by SDS-PAGE, reverse phase HPLC, and HPLC pep