Premium
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom