نتایج جستجو برای: kinetic inhibitor

تعداد نتایج: 295228  

2013
Judith Katharina Paulus Daniel Schlieper Georg Groth

The C4-photosynthetic carbon cycle is an elaborated addition to the classical C3-photosynthetic pathway, which improves solar conversion efficiency. The key enzyme in this pathway, phosphoenolpyruvate carboxylase, has evolved from an ancestral non-photosynthetic C3 phosphoenolpyruvate carboxylase. During evolution, C4 phosphoenolpyruvate carboxylase has increased its kinetic efficiency and redu...

Journal: :Clinical chemistry 1971
P J Garry

Dibucaine, used as a differential inhibitor with acetyl-, propionyl-, and butyr. ylthiocholine as substrate, clearly identified the “usual” and “atypical” serum cholinesterases. Succinylcholine was also used successfully as a differential inhibitor with butyrylthiocholine as substrate. Sodium fluoride, used as a differential inhibitor, gave conflicting results, depending on whether Tris or phos...

2009
X P Zheng P F Zhang Z J Liu E Y Wang

A novel model consisting of basic micro-processes has been developed on the basis of the classic diffusion theory. It is first time that the concept of exchange rate has been introduced and the growing process of surfactant-mediated epitaxial thin-film growth has been simulated with Kinetic Monte Carlo (KMC) technique. The results of simulation found that the exchange reaction of RLA model is a...

2016
Sanghamitra Mitra George Sheppard Jieyi Wang Brian Bennett Richard C. Holz Jeiyi Wang

Methionine aminopeptidases (MetAPs) represent a unique class of protease that is capable of the hydrolytic removal of an N-terminal methionine residue from nascent polypeptide chains. MetAPs are physiologically important enzymes; hence, there is considerable interest in developing inhibitors that can be used as anti-angiogenic and antimicrobial agents. A detailed kinetic and spectroscopic study...

Journal: :The Journal of biological chemistry 1984
G Campos V Guixé J Babul

The kinetic mechanisms of Escherichia coli phosphofructokinase-2 (Pfk-2) and of the mutant enzyme Pfk-2 were investigated. Initial velocity studies showed that both enzymes have a sequential kinetic mechanism, indicating that both substrates must bind to the enzyme before any products are released. For Pfk-2, the product inhibition kinetics was as follows: fructose-1,6-P2 was a competitive inhi...

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