Literature DB >> 464293

The nature of the random experimental error encountered when acetylcholine hydrolase and alcohol dehydrogenase are assayed.

I A Nimmo, S F Mabood.   

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Year:  1979        PMID： 464293     DOI： 10.1016/0003-2697(79)90358-0

Source DB:  PubMed          Journal:  Anal Biochem        ISSN： 0003-2697            Impact factor:   3.365


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  4 in total

1.  Error structure as a function of substrate and inhibitor concentration in enzyme kinetic experiments.

Authors:  B Mannervik; I Jakobson; M Warholm
Journal:  Biochem J       Date:  1986-05-01       Impact factor: 3.857

2.  Comparison of several non-linear-regression methods for fitting the Michaelis-Menten equation.

Authors:  L Matyska; J Kovár
Journal:  Biochem J       Date:  1985-10-01       Impact factor: 3.857

3.  An easy method for the determination of initial rates.

Authors:  S G Waley
Journal:  Biochem J       Date:  1981-03-01       Impact factor: 3.857

4.  Fitting of enzyme kinetic data without prior knowledge of weights.

Authors:  A Cornish-Bowden; L Endrenyi
Journal:  Biochem J       Date:  1981-03-01       Impact factor: 3.857
  4 in total

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