Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
about
Mechanism and kinetics of inducible nitric oxide synthase auto-S-nitrosation and inactivation.High performance enzyme kinetics of turnover, activation and inhibition for translational drug discovery.A novel approach to distinguish between enzyme mechanisms: quasi-steady-state kinetic analysis of the prostaglandin H synthase peroxidase reaction.Kinetics of an enzyme reaction in which both the enzyme-substrate complex and the product are unstable or only the product is unstable.Mean lifetime and first-passage time of the enzyme species involved in an enzyme reaction. Application to unstable enzyme systems.
P2860
Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
@en
Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
@nl
type
label
Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
@en
Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
@nl
prefLabel
Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
@en
Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
@nl
P2093
P2860
P356
P1433
P1476
Kinetic analysis of a Michaelis-Menten mechanism in which the enzyme is unstable.
@en
P2093
García-Cánovas F
Garrido-del Solo C
Havsteen BH
Varón-Castellanos R
P2860
P304
P356
10.1042/BJ2940459
P407
P478
294 ( Pt 2)
P577
1993-09-01T00:00:00Z