Enzymatic Reactions Involving Sulfate, Sulfite, Selenate, and Molybdate
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چکیده
منابع مشابه
Modeling Competitive Adsorption of Molybdate, Sulfate,and Selenate on g-Al2O3 by the Triple-Layer Model
Modeling Competitive Adsorption of Molybdate, Sulfate, and Selenate on γ -Al2O3 by the Triple-Layer Model Chung-Hsin Wu,∗ Shang-Lien Lo,∗ Cheng-Fang Lin,∗ and Chao-Yin Kuo†,1 ∗Graduate Institute of Environmental Engineering, National Taiwan University, 71 Chou-Shan Road, Taipei, 106, Taiwan; and †Institute and Department of Labor Relations, Chinese Culture University, 55 Hwa Kong Road, Shih-Lin...
متن کاملModeling competitive adsorption of molybdate, sulfate, selenate, and selenite using a Freundlich-type multi-component isotherm.
This study examined the interactions of MoO4(2-) + SO4(2-), MoO4(2-) + SeO4(2-), and MoO4(2-) + SeO3(2-) systems on gamma-Al2O3 to better understand the competitive adsorption of these anions in the natural environment. The Freundlich isotherms of anionic adsorption onto gamma-Al2O3 in single and binary solutes were also investigated to estimate the competition between these anions. Experimenta...
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Recent research has resulted in considerable modification of the earlier concept that enzymatic transamination was limited to reactions between alanine, aspartate, glutamate, and their or-keto analogues. Reactions leading to the reversible amination of the cY-keto analogues of many of the natural amino acids have been described (l-5), and there is also evidence that aldehyde groups may particip...
متن کاملYeast sulfate-reducing system. I. Reduction of sulfate to sulfite.
X35-APS-This substrate was synthesized from S%ulfur trioxide-pyridine complex and AMP by a method similar to that of Baddiley et al. (13) except for simplifications and modifications necessary for introduction of label. An alternat,ive method has been described by Reichard and Ringertz (14). Approximately 3.7 me of S35-HzS04 was dried at 80” in a reaction tube fitted with a ball joint and side ...
متن کاملEnzymatic Reactions
It has been argued that a substrate-induced conformational change involving the orientation of catalytic groups cannot affect the specificity for two substrates in an enzymatic system where the chemical step is rate limiting, because such an induced fit would alter the catalytic efficiency for both to an equal extent. To the contrary, the generalized induced-fit treatment described here shows t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1958
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)64689-7