IFCC Primary Reference Procedures for the Measurement of Catalytic Activity Concentrations of Enzymes at 37°C. Part 2. Reference Procedure for the Measurement of Catalytic Concentration of Creatine Kinase

Author(s):  
G. Schumann ◽  
R. Bonora ◽  
F. Ceriotti ◽  
P. Clerc-Renaud ◽  
C. A. Ferrero ◽  
...  
Author(s):  
G. Schumann ◽  
R. Aoki ◽  
C.A. Ferrero ◽  
G. Ehlers ◽  
G. Férard ◽  
...  

AbstractThis paper is the eighth in a series dealing with reference procedures for the measurement of catalytic activity concentrations of enzymes at 37°C and the certification of reference preparations. Other parts deal with: Part 1. The concept of reference procedures for the measurement of catalytic activity concentrations of enzymes; Part 2. Reference procedure for the measurement of catalytic concentration of creatine kinase; Part 3. Reference procedure for the measurement of catalytic concentration of lactate dehydrogenase; Part 4. Reference procedure for the measurement of catalytic concentration of alanine aminotransferase Part 5. Reference procedure for the measurement of catalytic concentration of aspartate aminotransferase Part 6. Reference procedure for the measurement of catalytic concentration of γ-glutamyltransferase; Part 7. Certification of four reference materials for the determination of enzymatic activity of γ-glutamyltransferase, lactate dehydrogenase, alanine aminotransferase and creatine kinase at 37°C. The procedure described here is deduced from the previously described 30°C IFCC reference method. Differences are tabulated and commented on.Clin Chem Lab Med 2006;44:1146–55.


1984 ◽  
Vol 30 (1) ◽  
pp. 143-144
Author(s):  
J C Hafkenscheid ◽  
C M van Dijk

Abstract We investigated the mechanism by which the three most commonly measured enzymes in erythrocytes are activated by their respective coenzymes by determining the catalytic activity concentrations of transketolase (EC 2.2.1.1), aspartate aminotransferase (EC 2.6.1.1), and glutathione reductase (EC 1.6.4.2) in relation to various substrate concentrations. We conclude that the underlying mechanisms by which the enzymes are activated are not the same.


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