Kinetics of α-chymotrypsin action. I. pH, solvent, and temperature effects

1967 ◽  
Vol 45 (5) ◽  
pp. 547-557 ◽  
Author(s):  
Harvey Kaplan ◽  
K. J. Laidler
Keyword(s):  
Dielectric Constant ◽  
Low Temperature ◽  
Temperature Effects ◽  
Methyl Esters ◽  
The Other ◽  
Kcal Mole ◽  
Influence Of Ph ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Ph Variations

An investigation has been made of the influence of pH on the kinetics of the α-chymotrypsin-catalyzed hydrolysis of N-acetyl-l-tyrosine ethyl ester, p-nitrophenyl acetate, and N-benzoyl-d- and -l-alanine methyl esters. From the pH variations of [Formula: see text], and [Formula: see text], it is deduced that in the free enzyme there are ionizing groups of pK 6.9 and 9.2. From the variation of these pK values with dielectric constant, it is concluded that, when protonated, one group is cationic and the other neutral. A temperature-dependence study was carried out on N–benzoyl-d- and -l-alanine methyl esters. The sharp break in the plot of log [Formula: see text] against 1/T is attributed to a rapid reversible denaturation of the enzyme at the higher temperatures. In the low-temperature region, the activation energies are ΔEL = 16.2 ± 0.3 kcal/mole and ΔED = 16.5 ± 0.6 kcal/mole.

Are some strains of subterranean clover (T. subterraneum) highly susceptible to low temperature stress?

1980 ◽  
Vol 20 (103) ◽  
pp. 197 ◽  
Author(s):  
RC Rossiter ◽  
WJ Collins
Keyword(s):  
Low Temperature ◽  
Temperature Stress ◽  
Growth Temperature ◽  
Temperature Effects ◽  
Subterranean Clover ◽  
The Other ◽  
Field Observations ◽  
Winter Dormancy ◽  
Plant Experiment ◽  
Temperature Interaction

Two experiments, one with spaced plants and the other with swards, were conducted in a controlled-temperature glasshouse at Perth, Western Australia. Three strains-Phillip Island, CPI 18293 and CPI 68043H-were selected on the basis of field observations of apparent very poor winter growth in rows, and tested against Tallarook as a control. The temperature treatments were 22/17� (day/night) and 12/7�C. In the spaced plant experiment (occupying the first 48 days of growth), temperature and strain effects were highly significant, but there was no indication of a strain x temperature interaction. In the sward experiment (from days 51 to 77) temperature effects were small; and in only one strain, Phillip Island, was the decline in tops growth due to low temperature greater (P< 0.05) than for Tallarook. The experiments failed to provide support for the so-called 'winter dormancy' phenomenon. Possible explanations for the discrepancy between the present findings and the field observations are given.

scholarly journals The kinetics of hydrolysis of some extended N-aminoacyl-l-arginine methyl esters by human plasma kallikrein. Evidence for subsites S2 and S3

1982 ◽  
Vol 203 (1) ◽  
pp. 149-153 ◽  
Author(s):  
P R Levison ◽  
G Tomalin
Keyword(s):  
Human Plasma ◽  
Methyl Esters ◽  
Plasma Kallikrein ◽  
Substrate Complex ◽  
Enzyme Substrate ◽  
Rate Limiting Step ◽  
Kinetics Of Hydrolysis ◽  
Rate Limiting ◽  
Kinetics Of ◽  
Hydrolysis Of

Subsites in the S2-S4 region were identified in human plasma kallikrein. Kinetic constants (kcat., Km) were determined for a series of seven extended N-aminoacyl-L-arginine methyl esters based on the C-terminal sequence of bradykinin (-Pro-Phe-Arg) or (Gly)n-Arg. The rate-limiting step for the enzyme-catalysed reaction was found to be deacylation of the enzyme. It was possible to infer that hydrogen-bonded interactions occur between substrate and the S2-S4 region of kallikrein. Insertion of L-phenylalanine at residue P2 demonstrates that there is also a hydrophobic interaction with subsite S2, which stabilizes the enzyme-substrate complex. The strong interaction demonstrated between L-proline at residue P3 and subsite S3 is of greatest importance in the selectivity of human plasma kallikrein. The purification of kallikrein from Cohn fraction IV of human plasma is described making use of endogenous Factor XIIf to activate the prekallikrein. Kallikreins I (Mr 91 000) and II (Mr 85 000) were purified 170- and 110-fold respectively. Kallikrein I was used for the kinetic work.

Low Temperature Deformation Kinetics of Ruthenium Aluminide Alloys

1998 ◽  
Vol 552 ◽  
Author(s):  
D. C. Lu ◽  
T. M. Pollock
Keyword(s):  
High Temperature ◽  
Low Temperature ◽  
Strain Rate ◽  
Rate Change ◽  
The Other ◽  
Temperature Deformation ◽  
Strain Rate Change ◽  
Deformation Kinetics ◽  
Ruthenium Aluminide ◽  
Kinetics Of

ABSTRACTThe kinetics of low temperature deformation were investigated in several different polycrystalline RuAl alloys with the use of strain rate change experiments at 77 K and 298 K. Compositions investigated include RuAl, RuAl+0.5%B, Ru51.5 A48.5, Ru52 Al48, RU53 A147+0.5%B, Ru54.5 Al45.5, and Ru52 Al43 Sc5. Flow stresses did not vary substantially with temperature between 77 K and 298 K. Rate sensitivities were low compared to other B2 compounds and similar in all compositions investigated. Analyses of dislocation substructures after low strain deformation were conducted. The deformation kinetics and substructural observations suggest a higher intrinsic deformability for RuAI alloys with respect to the other high temperature B2 aluminides.

The kinetics of the acid and alkaline hydrolysis of methyl fluoride in water

1952 ◽  
Vol 211 (1105) ◽  
pp. 254-265 ◽  
Keyword(s):  
Alkaline Hydrolysis ◽  
The Other ◽  
Methyl Halides ◽  
Methyl Fluoride ◽  
Rate Determining Step ◽  
Hydroxyl Ion ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Kinetic Features

The kinetics of the reaction of methyl fluoride with water and the hydroxyl ion have been determined experimentally at various concentrations and temperatures. The results are compared with the data available on the other methyl halides. The mechanism of the anionic reaction is discussed in terms of a hypothesis according to which the rate-determining step is the partial desolvation of the ion. This mechanism is extended to account also for the kinetic features of the hydrolysis.

THE NON-ENZYMATIC HYDROLYSIS OF ADENOSINE DIPHOSPHATE

1957 ◽  
Vol 35 (12) ◽  
pp. 1496-1503 ◽  
Author(s):  
K. A. Holbrook ◽  
Ludovic Ouellet
Keyword(s):  
Activation Energy ◽  
Aqueous Solution ◽  
Enzymatic Hydrolysis ◽  
Inorganic Phosphate ◽  
Adenosine Diphosphate ◽  
Hydrogen Ions ◽  
Kcal Mole ◽  
First Order ◽  
Kinetics Of ◽  
Hydrolysis Of

The kinetics of the non-enzymatic hydrolysis of adenosine diphosphate in aqueous solution have been studied at pH 3.5 to 10.5 and temperatures from 80° to 95 °C. The reaction has been followed by measuring colorimetrically the inorganic phosphate liberated according to the over-all reaction[Formula: see text]The reaction has been found to be first order with respect to ADP concentration and to be catalyzed by hydrogen ions. From rate studies at pH 8.0 an activation energy of 24.2 kcal./mole was derived. A mechanism is proposed to account for the observed facts and the mechanism for the hydrolysis of adenosine triphosphate is also discussed.

scholarly journals Индуцированный фазовый переход в монокристаллических твердых растворах PbMg-=SUB=-1/3-=/SUB=-Nb-=SUB=-2/3-=/SUB=-O-=SUB=-3-=/SUB=--29PbTiO-=SUB=-3-=/SUB=- и PbZn-=SUB=-1/3-=/SUB=-Nb-=SUB=-2/3-=/SUB=-O-=SUB=-3-=/SUB=--9PbTiO-=SUB=-3-=/SUB=-: сходство и различие

2021 ◽  
Vol 63 (11) ◽  
pp. 1880
Author(s):  
Л.С. Камзина
Keyword(s):  
Phase Transition ◽  
Dielectric Constant ◽  
Low Temperature ◽  
Electric Fields ◽  
Delay Time ◽  
Optical Transmission ◽  
Ferroelectric Phase ◽  
Morphotropic Phase Transition ◽  
Macroscopic Polarization ◽  
Kinetics Of

The kinetics of the induced phase transition in single-crystal relaxor solid solutions PbMg1 / 3Nb2 / 3O3-29PbTiO3 and PbZn1 / 3Nb2 / 3O3-9PbTiO3 is studied when an electric field is applied along the [001] direction. At temperatures below the temperature of the morphotropic phase transition, the changes in the dielectric constant and optical transmission in electric fields are studied. It is shown that the decrease in optical transmission with time is associated only with a change in the sizes of nanoregions during the phase transition. It was found that the induced phase transition proceeds differently in these crystals. In PMN-29PT crystals, the formation of ferroelectric phases and the rapid establishment of macroscopic polarization are preceded by a certain delay time, while in PZN-9PT crystals, the ferroelectric phase is induced immediately after the application of the field without a delay time. The results obtained are explained by the different structures of the low-temperature phases in these compounds. Key words: ferroelectricity, relaxors, induced phase transition.

scholarly journals The Contractile and Control Sites of Natural Actomyosin

1967 ◽  
Vol 50 (10) ◽  
pp. 2421-2435 ◽  
Author(s):  
Harvey M. Levy ◽  
Elizabeth M. Ryan
Keyword(s):  
Control System ◽  
Driving Force ◽  
Inhibitory Action ◽  
Atp Hydrolysis ◽  
The Other ◽  
Contractile System ◽  
Contraction And Relaxation ◽  
And Control ◽  
Kinetics Of ◽  
Hydrolysis Of

The various contractile and control sites of natural actomyosin gel were studied by comparing the kinetics of ATP hydrolysis with those of gel contraction, measured as an increase in turbidity. Contraction of actomyosin gel seems to require the cooperative reaction of ATP (with Mg) at two different sites. One of these sites catalyzes the hydrolysis of ATP and most probably contributes the driving force for contraction; the binding of ATP to the other site appears to break certain links that retard movement of the gel components. At limiting concentrations of ATP, the rate of contraction seems to depend on the rate of breaking these links as well as on the rate of ATP hydrolysis. But when both sites are saturated, the rate of contraction appears to be limited only by the rate of ATP hydrolysis. In addition to these two contractile sites, there are also two different control sites. At one, the relaxing site, the binding of ATP with Mg inhibits ATP hydrolysis and gel contraction. At the other, the binding of calcium activates contraction by overcoming the inhibitory action of Mg and ATP at the relaxing site. This control system—inhibition by substrate and disinhibition by calcium—can be selectively inactivated by heat and reactivated by dithiothreitol, a disulfide-reducing agent. These observations on the isolated contractile system are discussed in relation to the contraction and relaxation of muscle.

THE TRYPSIN CATALYZED HYDROLYSIS OF p-NITROPHENYL ACETATE

1959 ◽  
Vol 37 (4) ◽  
pp. 751-759 ◽  
Author(s):  
James A. Stewart ◽  
Ludovic Ouellet
Keyword(s):  
Active Site ◽  
Initial Rate ◽  
Competitive Inhibition ◽  
Early Stage ◽  
Stopped Flow ◽  
Hydrogen Ions ◽  
Experimental Conditions ◽  
Influence Of Ph ◽  
Kinetics Of ◽  
Hydrolysis Of

The hydrolysis of p-nitrophenyl acetate (NPA) by trypsin has been investigated in the early stage of the reaction using stopped-flow techniques. The influence of pH on the initial rate suggests competitive inhibition of the active site of the enzyme by hydrogen ions. The dissociation constant of the enzyme obtained from the kinetics of this reaction (pK = 6.9) indicates possible catalysis by an ammo group or an imidazole group of the enzyme. Lysine methyl ester as an analogue of the enzyme catalyzes the hydrolysis of NPA under similar experimental conditions. The results are described in terms of an assumed mechanism and the nature of the catalytic site is discussed.

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