Kinetics of the Tryptic Hydrolysis of the Oxidized B Chain of Bovine Insulin*

Biochemistry ◽  
1967 ◽  
Vol 6 (1) ◽  
pp. 215-224 ◽  
Author(s):  
Su-Sun Wang ◽  
Frederick H. Carpenter
Keyword(s):  
Bovine Insulin ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Tryptic Hydrolysis

scholarly journals Kinetics of the Tryptic Hydrolysis of Zinc-free Bovine Insulin

1969 ◽  
Vol 244 (20) ◽  
pp. 5537-5543
Author(s):  
Su-Sun Wang ◽  
Frederick H. Carpenter
Keyword(s):  
Bovine Insulin ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Tryptic Hydrolysis

scholarly journals Kinetics of tryptic hydrolysis of the arginine-valine bond in folded and unfolded ribonuclease T1

1984 ◽  
Vol 219 (2) ◽  
pp. 411-417 ◽  
Author(s):  
C N Pace ◽  
A J Barrett
Keyword(s):  
Kinetic Studies ◽  
Peptide Bond ◽  
Small Peptides ◽  
Ribonuclease T1 ◽  
Chemically Modified ◽  
Steady State Kinetic ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
State Kinetic ◽  
Tryptic Hydrolysis

We have used ribonuclease T1 and its chemically modified derivatives as substrates, and trypsin as proteinase, to investigate the kinetics of proteolysis of a specific peptide bond in the folded and unfolded conformations of a protein. Steady-state kinetic studies showed that Km = 0.27 mM and Kcat. = 2.45 s-1 for the tryptic hydrolysis of the Arg(77)-Val(78) peptide bond in unfolded ribonuclease T1. This Km is somewhat lower than, and the kcat. value similar to, values found for the tryptic hydrolysis of comparable bonds in small peptides. Our data for the initial velocity of hydrolysis of the Arg(77)-Val(78) bond in a solution of the folded protein indicate that the bond is at least 1700 times less rapidly hydrolysed in the folded than in the unfolded conformation of ribonuclease T1, and do not exclude the possibility that the bond is completely resistant to hydrolysis in the folded protein.

Tryptic hydrolysis of bovine αS2-casein: identification and release kinetics of peptides

2003 ◽  
Vol 13 (1) ◽  
pp. 15-27 ◽  
Author(s):  
J. Tauzin ◽  
L. Miclo ◽  
S. Roth ◽  
D. Mollé ◽  
J.-L. Gaillard
Keyword(s):  
Release Kinetics ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Tryptic Hydrolysis

scholarly journals THE KINETICS OF ENZYME REACTIONS: SCHÜTZ'S LAW

1930 ◽  
Vol 13 (3) ◽  
pp. 323-334 ◽  
Author(s):  
E. A. Moelwyn-Hughes ◽  
J. Pace ◽  
W. C. M. Lewis
Keyword(s):  
Experimental Results ◽  
Mass Action ◽  
Law Of Mass Action ◽  
Enzyme Reactions ◽  
Adsorption Theory ◽  
The Law ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Tryptic Hydrolysis ◽  
Made In

1. A review of the applicability of Schütz's Law to enzymic reactions is given. 2. The theoretical deductions of the Law, (a) on the basis of the law of mass action, (b) on the basis of the adsorption theory, are given and the significance of the assumptions made in these deductions pointed out. 3. It is shown that the true critical increment for an enzymic reaction is equal to twice the critical increment calculated from the Schütz constant ks, if the heat of decomposition of the enzyme-products complex be neglected. 4. Experiments are described on the tryptic hydrolysis of casein at 30°C. and 404C. The foregoing considerations are applied to the experimental results obtained.

Influence of medium on alkaline hydrolysis of succinic acid monomethyl and monopropyl esters

1980 ◽  
Vol 45 (11) ◽  
pp. 2873-2882
Author(s):  
Vladislav Holba ◽  
Ján Benko
Keyword(s):  
Succinic Acid ◽  
Kinetic Parameters ◽  
Alkaline Hydrolysis ◽  
Specific Interactions ◽  
Nonaqueous Media ◽  
The Media ◽  
Kinetics Of ◽  
Hydrolysis Of

The kinetics of alkaline hydrolysis of succinic acid monomethyl and monopropyl esters were studied in mixed aqueous-nonaqueous media at various temperatures and ionic strengths. The results of measurements are discussed in terms of electrostatic and specific interactions between the reactants and other components of the reaction mixture. The kinetic parameters in the media under study are related to the influence of the cosolvent on the solvation sphere of the reactants.

Belousov–Zhabotinskii type oscillation reaction with glycerol and kinetics of reactions between the system components

1987 ◽  
Vol 52 (10) ◽  
pp. 2375-2382 ◽  
Author(s):  
Ľubica Adamčíková ◽  
Peter Ševčík
Keyword(s):  
Oscillation System ◽  
Chemical Oscillations ◽  
Oscillation Reaction ◽  
Reaction Solution ◽  
System Components ◽  
Probable Source ◽  
Belousov Zhabotinskii Reaction ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Type Oscillation

Glycerol causes chemical oscillations in Belousov-Zhabotinskii reaction in a closed system as well as in a reaction solution bubbled with nitrogen. Since the oxidation of glycerol with bromate ions does not proceed autocatalytically and bromine in the oxidation state 0 or +1 in the absence of light does not react with glycerol, hydrolysis of bromine is the probable source of bromide ions in the studied oscillation system.

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