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enzyme activity
The enzyme exists mainly in soluble form; the activity of membrane-associated enzyme is 7-25% of soluble enzyme activity depending on tissue type.
      
It is shown that each form of cytochrome P45017α is characterized by a specific profile of enzyme activity and dependence of 17,20-lyase reaction on the presence of cytochrome b5 in the reaction mixture.
      
Inorganic phosphate prevents and azide promotes a decline of the enzyme activity during ATP hydrolysis.
      
As compared to riboflavin, a tenfold excess of its analog 7,8-dimethyl-10-(O-methylacetoxime)-isoalloxazine decreased the enzyme activity by 30%.
      
Other analogs of riboflavin failed to markedly affect the enzyme activity.
      
The enzyme activity in the presence of bivalent metal ions decreases in the series (Ca2+ + Mg2+) >amp;gt; Mn2+ = (Ca2+ + Mn2+) >amp;gt; (Mg2+ + EGTA) >amp;gt; Ca2+.
      
The enzyme activity in the presence of bivalent metal ions decreases in the series (Ca2+ + Mn2+) >amp;gt; (Ca2+ + Mg2+) >amp;gt; Mn2+ >amp;gt; (Mg2+ + EGTA).
      
Both enzyme activities are inhibited by excess biliverdin IXα, but the NADPH-dependent enzyme activity is far more susceptible.
      
In the present paper, the effects of dimethyl sulfoxide on the enzyme activity for the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) have been studied.
      
Another mutant enzyme obtained by mutation of Glu20 in the motif to Ser, Leu, Thr, Gln, Ala, or Val had an enzyme activity of less than 1% of the wild type.
      
These results clearly indicated that Trp17 and Glu20 are essential for the enzyme activity.
      
Stoichiometry studies by Tsou's method showed that among the cysteine residues available for OPTA modification in the enzyme, only one was essential for the enzyme activity.
      
In this work, the effects of dioxane on the enzyme activity for the hydrolysis of p-nitrophenyl-N-acetyl-β-D-glucosaminide from the prawn (Penaeus vannamei) have been studied.
      
Stoichiometry studies by Tsou's method showed that among the cysteine residues available for OPTA modification in the enzyme, only one was essential for the enzyme activity.
      
In this work, the effects of dioxane on the enzyme activity for the hydrolysis of p-nitrophenyl-N-acetyl-β-D-glucosaminide from the prawn (Penaeus vannamei) have been studied.
      
The enzyme activity is stimulated by 2.5 mM Mg2+ and 0.1 mM Co2+ 15- and 31-fold, respectively.
      
The system for enzyme activity detection was optimized.
      
o-NPF is the most effective inhibitor of the enzyme activity with Ki value of 0.41 mM.
      
The enzyme activity eluted from a Sephacryl S-300 column in a single peak associated with a protein of molecular weight ~300 kD and a Stokes radius of 5.4 nm.
      
This interaction is fully reversed by EDTA and results in a partial inhibition of the enzyme activity (50-90%,depending on preparation) with an effective Ki of ~10 μM.
      
 

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