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Although most of enzyme catalytic reactions are specific, the amperometric detection of the enzymatic reaction products is largely nonselective.
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However, due to the complexity of the enzyme mixture, the enzymes interaction with and interference from the substrate and a lack of specific methods to follow the distribution of individual enzymes during hydrolysis, most of enzyme-substrate interaction studies have used purified enzymes and pure cellulose model substrates.
Excess Pyr disturbs the balance of enzyme partition and shifts most of enzymes to the valine biosynthesis.
However, the enzyme activator substance APMA altered the size of the band, indicating that most of the enzyme was expressed as a pro-form [ 28].
Most of the enzyme structure has fixed three-dimensional conformation.
In this study, we constructed a mini binary vector (4 kb), pBD003, in which most of restriction enzyme sites on the plasmid backbone were removed.
Most of these enzyme systems function by alternating between the oxidized and reduced state of the coenzymes NAD-NADH and NADP-NADPH.
Most of the enzyme was immobile, the mobile fraction being only 36% (Fig. 2C, G and Table 1).
Most of the enzyme inhibition studies used iAsIII and some used organic arsenicals, particularly phenylarsine oxide (PAO).
Most of these enzymes have been divided into families in a classification system for Carbohydrate Active enZymes (CAZy, http://www.cazy.org) [ 10].
The evolutionary trade-offs observed by Tcherkez et al. are consistent with the occurrence of most of these enzymes.
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