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PMID: 4464860 Published · ppublish English Journal Article

A new method for determining the Michaelis constant.

The Biochemical journal ·Vol. 143 ·No. 1 ·1974-10-00 ·Pages 93-5

De Merino FM

Abstract

A new method is described for evaluating the parameters K(m) and V in the Michaelis-Menten equation, and is illustrated with experimental data from the literature.

MeSH Terms
Kinetics Mathematics Optical Rotation Sucrose
Chemicals
Sucrose
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
De Merino F M
References (3)
3 references, click to expand
  1. Statistical analysis of enzymic steady-state rate data.
    C R Trav Lab Carlsberg. 1961;32:185-214 PMID: 14451942
  2. Statistical estimations in enzyme kinetics.
    Biochem J. 1961 Aug;80:324-32 PMID: 13785321
  3. Studies on plant amylases: The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley.
    Biochem J. 1932;26(5):1406-21 PMID: 16744959
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1430093
Published
1974-10-00
Pages
93-5
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1168356
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1430093 PMC Full Text View journal details
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