The interaction of amino acids with o-phthaldialdehyde: A kinetic study and spectrophotometric assay of the reaction product

1980 ◽  
Vol 101 (1) ◽  
pp. 188-195 ◽  
Author(s):  
Vytas-J.K. Švedas ◽  
Igor J. Galaev ◽  
Ivan L. Borisov ◽  
Ilya V. Berezin
Keyword(s):  
Amino Acids ◽  
Kinetic Study ◽  
Spectrophotometric Assay

scholarly journals Kinetics of a self-amplifying substrate cycle: ADP–ATP cycling assay

2000 ◽  
Vol 350 (1) ◽  
pp. 237-243 ◽  
Author(s):  
Edelmira VALERO ◽  
Ramón VARÓN ◽  
Francisco GARCÍA-CARMONA
Keyword(s):  
Lactate Dehydrogenase ◽  
Kinetic Study ◽  
Pyruvate Kinase ◽  
Adenylate Kinase ◽  
Reaction Medium ◽  
Spectrophotometric Assay ◽  
Background Signal ◽  
Cyclic System ◽  
Exponential Increase ◽  
Kinetics Of

A kinetic study of an ATP–ADP amplification cyclic system involving the enzymes adenylate kinase, pyruvate kinase and l-lactate dehydrogenase has been made. The stoichiometry of the cycle is 2:1, because two molecules of ADP are synthesized from one each of ATP and AMP, and one molecule of ADP is converted back into one of ATP at each turn of the cycle. This results in a continuous exponential increase in the concentrations of ATP and ADP in the reaction medium, according to the equations obtained. This is therefore a substrate cycle that amplifies itself, the cycling rate increasing continuously with time. The background signal of the reagent was reduced by using apyrase to degrade ATP and ADP in the reagent, permitting detection limits as low as 16pmol of ATP and/or ADP in a continuous spectrophotometric assay.

Oxidation of amino acids by peroxomonophosphoric acid?a kinetic study

1991 ◽  
Vol 23 (4) ◽  
pp. 345-359 ◽  
Author(s):  
Ganesh P. Panigrahi ◽  
Ramesh C. Paichha
Keyword(s):  
Amino Acids ◽  
Kinetic Study

Kinetic study of amino acids inhibition potential of Glycine and l -leucine on the ethane hydrate formation

2015 ◽  
Vol 26 ◽  
pp. 819-826 ◽  
Author(s):  
Shiva Abbasian Rad ◽  
Khadije Rostami Khodaverdiloo ◽  
Maryam Karamoddin ◽  
Farshad Varaminian ◽  
Kiana Peyvandi
Keyword(s):  
Amino Acids ◽  
Kinetic Study ◽  
Hydrate Formation

scholarly journals Mechanistic study on substitution reaction of a citrato(p-cymene)Ru(ii) complex with sulfur-containing amino acids

RSC Advances ◽  
2019 ◽  
Vol 9 (43) ◽  
pp. 25177-25183
Author(s):  
Sen-ichi Aizawa ◽  
Kohei Takizawa ◽  
Momoko Aitani
Keyword(s):  
Amino Acids ◽  
Reaction Mechanism ◽  
Kinetic Study ◽  
Substitution Reaction ◽  
Mechanistic Study ◽  
Sulfur Containing

Thorough kinetic study revealed characteristics of the reaction mechanism for arene ruthenium(ii) complexes with bio-related ligands.

scholarly journals Starch-Binding Domain Affects Catalysis in Two Lactobacillus α-Amylases

2005 ◽  
Vol 71 (1) ◽  
pp. 297-302 ◽  
Author(s):  
R. Rodr�guez-Sanoja ◽  
B. Ruiz ◽  
J. P. Guyot ◽  
S. Sanchez
Keyword(s):  
Amino Acids ◽  
Kinetic Study ◽  
Lactobacillus Plantarum ◽  
Tandem Repeats ◽  
Binding Domain ◽  
Sequence Identity ◽  
Adsorption Capacities ◽  
Lactobacillus Amylovorus ◽  
Amylase Genes ◽  
A Minor

ABSTRACT A new starch-binding domain (SBD) was recently described in α-amylases from three lactobacilli (Lactobacillus amylovorus, Lactobacillus plantarum, and Lactobacillus manihotivorans). Usually, the SBD is formed by 100 amino acids, but the SBD sequences of the mentioned lactobacillus α-amylases consist of almost 500 amino acids that are organized in tandem repeats. The three lactobacillus amylase genes share more than 98% sequence identity. In spite of this identity, the SBD structures seem to be quite different. To investigate whether the observed differences in the SBDs have an effect on the hydrolytic capability of the enzymes, a kinetic study of L. amylovorus and L. plantarum amylases was developed, with both enzymes acting on several starch sources in granular and gelatinized forms. Results showed that the amylolytic capacities of these enzymes are quite different; the L. amylovorus α-amylase is, on average, 10 times more efficient than the L. plantarum enzyme in hydrolyzing all the tested polymeric starches, with only a minor difference in the adsorption capacities.

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