2004
DOI: 10.1016/s0032-9592(02)00246-7
|View full text |Cite
|
Sign up to set email alerts
|

A vector method of representation of enzymic reactions

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

0
3
0
1

Year Published

2007
2007
2014
2014

Publication Types

Select...
5

Relationship

0
5

Authors

Journals

citations
Cited by 9 publications
(4 citation statements)
references
References 24 publications
0
3
0
1
Order By: Relevance
“…где [I] -концентрация ингибитора [24]. Ис-пользование этой формулы дает значение K I = 53 мкМ -величину одного порядка с при-водимыми в литературе K I ТНЩФ (K I = 6,6-320 мкМ) [20,[25][26][27].…”
Section: результаты и обсуждениеunclassified
“…где [I] -концентрация ингибитора [24]. Ис-пользование этой формулы дает значение K I = 53 мкМ -величину одного порядка с при-водимыми в литературе K I ТНЩФ (K I = 6,6-320 мкМ) [20,[25][26][27].…”
Section: результаты и обсуждениеunclassified
“…A vector method of representation of the enzymatic reaction in the three-dimensional K m V I system of rectangular coordinates (Figure 1) shows that a ratio of length of the L vector projection of the reaction under study on the Pa, i semiaxis of molar concentrations of inhibitor (or activator) to dimensionless positive difference of the coordinates of this vector orthogonal projection on the basic σ 0 plane of the examined coordinate system is an equation for calculation of the K i constants of enzyme inhibition (or K a constants of enzyme activation), depending on what effect is being studied [4,5].…”
Section: Deduction Of Equations For Calculation Of Constants Of Biparmentioning
confidence: 99%
“…• C [4]. The final concentrations of pNPP varied between 2.94 × 10 −5 and 9.8 × 10 −5 M and concentration of canine alkaline phosphatase was kept constant at 1.13 μg.…”
Section: Enzyme Activity Assaymentioning
confidence: 99%
“…Kinetic parameters of ALDH (Kt, half-reaction time of the enzyme substrate; V max , maximum rate of reaction product accumulation under complete consumption of the substrate; and V max /Kt, coeffi cient of the catalytic effi ciency for the enzyme reaction) were evaluated from primary data [8]. Kinetic parameters were recorded [3]. The results were analyzed by Student's t test (BIOSTAT software) [1].…”
mentioning
confidence: 99%