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Über die Hemmung der Leber‐ und der Muskelaldolase durch Glycerinaldehyd‐3‐phosphat. 15. Mitteilung über Aldolasen [1]
Author(s) -
Hotz R.,
Leuthardt F.
Publication year - 1968
Publication title -
helvetica chimica acta
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.74
H-Index - 82
eISSN - 1522-2675
pISSN - 0018-019X
DOI - 10.1002/hlca.19680510613
Subject(s) - chemistry , aldolase a , kinetics , dissociation constant , ternary complex , enzyme , substrate (aquarium) , stereochemistry , biochemistry , physics , receptor , quantum mechanics , oceanography , geology
1 The kinetics of the inhibition of rabbit muscle and liver aldolase by DL ‐glyceraldehyde‐3‐phosphate have been studied. 2 The inhibition is of the non‐competitive type. 3 The ternary enzyme‐substrate‐GAP‐complex shows a residual enzyme activity, muscle aldolase‐FDP showing the highest and liver aldolase‐F‐1‐P the lowest activity. 4 The dissociation constant K 0 ′ (ESI ⇄ ES+I) has been determined on the assumption of quasi‐equilibrium kinetics.