Experimental determination of kinetic parameters of methanol biodegradation in biofilters packed with inert and organic materials

2009 ◽  
Vol 85 (3) ◽  
pp. 404-409 ◽  
Author(s):  
Antonio Avalos Ramirez ◽  
Jonathan Deschamps ◽  
J. Peter Jones ◽  
Michèle Heitz
Keyword(s):  
Experimental Determination ◽  
Kinetic Parameters ◽  
Organic Materials

Experimental determination of kinetic parameters for crystallizing amorphous NiTi thin films

2005 ◽  
Vol 87 (11) ◽  
pp. 114102 ◽  
Author(s):  
Hoo-Jeong Lee ◽  
Hai Ni ◽  
David T. Wu ◽  
Ainissa G. Ramirez
Keyword(s):  
Thin Films ◽  
Experimental Determination ◽  
Kinetic Parameters

scholarly journals Identification and dynamics of the human ZDHHC16-ZDHHC6 palmitoylation cascade

eLife ◽  
2017 ◽  
Vol 6 ◽  
Author(s):  
Laurence Abrami ◽  
Tiziano Dallavilla ◽  
Patrick A Sandoz ◽  
Mustafa Demir ◽  
Béatrice Kunz ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Mathematical Modelling ◽  
Experimental Determination ◽  
Kinetic Parameters ◽  
Turnover Rate ◽  
Data Driven ◽  
Lipid Modification ◽  
Site Specific

S-Palmitoylation is the only reversible post-translational lipid modification. Knowledge about the DHHC palmitoyltransferase family is still limited. Here we show that human ZDHHC6, which modifies key proteins of the endoplasmic reticulum, is controlled by an upstream palmitoyltransferase, ZDHHC16, revealing the first palmitoylation cascade. The combination of site specific mutagenesis of the three ZDHHC6 palmitoylation sites, experimental determination of kinetic parameters and data-driven mathematical modelling allowed us to obtain detailed information on the eight differentially palmitoylated ZDHHC6 species. We found that species rapidly interconvert through the action of ZDHHC16 and the Acyl Protein Thioesterase APT2, that each species varies in terms of turnover rate and activity, altogether allowing the cell to robustly tune its ZDHHC6 activity.

scholarly journals Identification and dynamics of the DHHC16-DHHC6 palmitoylation cascade

2017 ◽  
Author(s):  
Laurence Abrami ◽  
Tiziano Dallavilla ◽  
Patrick A. Sandoz ◽  
Mustafa Demir ◽  
Béatrice Kunz ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Mathematical Modelling ◽  
Experimental Determination ◽  
Kinetic Parameters ◽  
Turnover Rate ◽  
Data Driven ◽  
Lipid Modification ◽  
Site Specific

ABSTRACTS-Palmitoylation is the only reversible post-translational lipid modification. Knowledge about the DHHC family of palmitoyltransferases is very limited. Here we show that mammalian DHHC6, which modifies key proteins of the endoplasmic reticulum, is controlled by an upstream palmitoyltransferase, DHHC16, revealing the first palmitoylation cascade. Combination of site specific mutagenesis of the three DHHC6 palmitoylation sites, experimental determination of kinetic parameters and data-driven mathematical modelling allowed us to obtain detailed information on the 8 differentially palmitoylated DHHC6 species. We found that species rapidly interconvert through the action of DHHC16 and the Acyl Protein Thioesterase APT2, that each species varies in terms of turnover rate and activity, altogether allowing the cell to robustly tune its DHHC6 activity.

Modeling particle inflation from poly(amic acid) powdered precursors. III. Experimental determination of kinetic parameters

2008 ◽  
Vol 48 (3) ◽  
pp. 617-626 ◽  
Author(s):  
Camilo I. Cano ◽  
Meaghan L. Clark ◽  
Thein Kyu ◽  
R. Byron Pipes
Keyword(s):  
Experimental Determination ◽  
Kinetic Parameters ◽  
Amic Acid

Experimental determination of a state equation for dissipative granular gases

1999 ◽  
Vol 96 (6) ◽  
pp. 1111-1116 ◽  
Author(s):  
E. Falcon ◽  
S. Fauve ◽  
C. Laroche
Keyword(s):  
Experimental Determination ◽  
State Equation ◽  
Granular Gases

MEASUREMENT OF STEROID BINDING PROTEINS

1970 ◽  
Vol 65 (1_Suppl) ◽  
pp. S104-S121 ◽  
Author(s):  
E. E. Baulieu ◽  
J. P. Raynaud ◽  
E. Milgrom
Keyword(s):  
Kinetic Parameters ◽  
Binding Proteins ◽  
Binding Specificity ◽  
Binding Parameters ◽  
Target Organs ◽  
Biological Mixtures ◽  
Steroid Binding Proteins ◽  
Steroid Binding ◽  
Steroid Binding Protein

ABSTRACT A brief review of the characteristics of steroid binding proteins found in the plasma and in some target organs is presented, followed by some general remarks on binding »specificity« and binding parameters. Useful techniques for measuring binding parameters at equilibrium are reported, both those which keep the equilibrium intact and those which implicate its disruption. A concept is developed according to which the determination of a specific steroid binding protein is based on the »differential dissociation« of the several steroid binding complexes present in most biological mixtures. Methods which allow determination of the kinetic parameters of the binding systems are also presented. Various representations of the binding and therefore different modes of graphic representation and calculation are discussed, including the recent »proportion graph« method.

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