scholarly journals A two-state model of an enzyme with an allosteric regulatory site capable of metabolizing the regulatory ligand. Simplified mathematical treatments of transient and steady state kinetics of an activator and its competitive inhibition as applied to adenylyl cyclases.

1980 ◽  
Vol 255 (8) ◽  
pp. 3552-3557
Author(s):  
L. Birnbaumer ◽  
C.F. Bearer ◽  
R. Iyengar
Keyword(s):  
Steady State ◽  
Competitive Inhibition ◽  
State Model ◽  
Adenylyl Cyclases ◽  
Regulatory Site ◽  
Steady State Kinetics ◽  
Two State Model ◽  
Kinetics Of ◽  
Transient And Steady State

scholarly journals Transient and Steady-state Kinetics of the Oxidation of Substituted Benzoic Acid Hydrazides by Myeloperoxidase

1999 ◽  
Vol 274 (14) ◽  
pp. 9494-9502 ◽  
Author(s):  
Ursula Burner ◽  
Christian Obinger ◽  
Martina Paumann ◽  
Paul G. Furtmüller ◽  
Anthony J. Kettle
Keyword(s):  
Steady State ◽  
Benzoic Acid ◽  
Steady State Kinetics ◽  
Kinetics Of ◽  
Transient And Steady State

Polarographic studies on renaturation of urea-denatured human serum albumin

1989 ◽  
Vol 54 (2) ◽  
pp. 536-543 ◽  
Author(s):  
Josef Chmelík ◽  
Pavel Anzenbacher ◽  
Vítěz Kalous
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Irreversible Process ◽  
State Model ◽  
Native Protein ◽  
Main Components ◽  
Two State Model ◽  
Kinetics Of

The renaturation of the two main components of human serum albumin, i.e. of mercaptalbumin and nonmercaptalbumin, was studied polarographically. It has been demonstrated that renaturation of both proteins after 1-min denaturation in 8M urea is reversible. By contrast, renaturation after 200 min denaturation in 8M urea is an irreversible process; the characteristics of renatured mercaptalbumin differ more from the properties of the native protein than the characteristics of nonmercaptalbumin. The studies of the kinetics of renaturation of both proteins have shown that the renaturation can be represented by a two-state model. This means that the existence of stable intermediary products during the renaturation process was not determined polarographically.

Sign in / Sign up

Export Citation Format

Share Document