Validity of a 'steady-state' treatment of inactivation kinetics.

Validity of a 'steady-state' treatment of inactivation kinetics.

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http://www.wikidata.org/entity/Q41491474
Structural basis for the insensitivity of a serine enzyme (palmitoyl-protein thioesterase) to phenylmethylsulfonyl fluorideSubstrate-derived two-protonic-state electrophiles as sensitive kinetic specificity probes for cysteine proteinases. Activation of 2-pyridyl disulphides by hydrogen-bondingKinetics of protein modification reactions.Computer simulations of the kinetics of irreversible enzyme inhibition by an unstable inhibitor.The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactionsExperimental approach to the kinetic study of unstable site-directed irreversible inhibitors: kinetic origin of the apparent positive co-operativity arising from inactivation of trypsin by p-amidinophenylmethanesulphonyl fluoride.Some classical errors in the kinetic analysis of enzyme reactions
P2860

Validity of a 'steady-state' treatment of inactivation kinetics.

Item
http://www.wikidata.org/entity/Q41491474
description
1979 nî lūn-bûn
@nan
1979年の論文
@ja
1979年論文
@yue
1979年論文
@zh-hant
1979年論文
@zh-hk
1979年論文
@zh-mo
1979年論文
@zh-tw
1979年论文
@wuu
1979年论文
@zh
1979年论文
@zh-cn
name
Validity of a 'steady-state' treatment of inactivation kinetics.
@en
type
label
Validity of a 'steady-state' treatment of inactivation kinetics.
@en
prefLabel
Validity of a 'steady-state' treatment of inactivation kinetics.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Validity of a 'steady-state' treatment of inactivation kinetics.
@en
P2093
P2860
P304
P31
P356
10.1111/J.1432-1033.1979.TB12834.X
P407
P433
P478
P577
P698