Literature DB >> 7387626

Graphical determination of pK values of the active-site groups of enzymes. An analysis of the bell-shaped curves.

O Parkash, I S Bhatia.   

Abstract

Descriptions are given for the graphical determination of molecular pK values from the curves of logV and p(Km/V) against pH. The arguments are based on the model dissociation equilibria LAL in equilibrium (AL + LA) in equilibrium A, where A denotes a molecule having two binding sites for a ligand L.

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Year:  1980        PMID: 7387626      PMCID: PMC1161437          DOI: 10.1042/bj1850609

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  3 in total

1.  PH-dependence of the steady-state rate of a two-step enzymic reaction.

Authors:  K Brocklehurst; H B Dixon
Journal:  Biochem J       Date:  1976-04-01       Impact factor: 3.857

2.  On the interpretation of the pH variation of the maximum initial velocity of an enzyme-catalyzed reaction.

Authors:  R A ALBERTY; V MASSEY
Journal:  Biochim Biophys Acta       Date:  1954-03

3.  Negatively co-operative ligand binding.

Authors:  H B Dixon; K F Tipton
Journal:  Biochem J       Date:  1973-08       Impact factor: 3.857

  3 in total
  1 in total

1.  Regulatory properties of 14-day embryo and adult hen heart AMP-deaminase; the influence of pH on the enzyme activity.

Authors:  K Kaletha
Journal:  Experientia       Date:  1984-03-15
  1 in total

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