Kinetic characterization of an enzymatic irreversible inhibition measured in the presence of coupling enzymes. The inhibition of adenosine triphosphatase from sarcoplasmic reticulum by fluorescein isothiocyanate.
A kinetic study of the irreversible inhibition of an enzyme measured in the presence of a coupling enzyme system has been carried out to assess the type of mechanism of the irreversible inhibition. By using the algebraic criteria proposed here it should be possible to discriminate between these mechanisms and to calculate their corresponding kinetic constants. An experimental design has been developed and applied to fluorescein isothiocyanate as inhibitor of the ATPase activity from sarcoplasmic reticulum.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors*; D016650:Fluorescein-5-isothiocyanate; D005452:Fluoresceins / Q000494:pharmacology*; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D011770:Pyruvate Kinase / Q000378:metabolism; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*; D013861:Thiocyanates / Q000494:pharmacology*
D005452:Fluoresceins; D013861:Thiocyanates; D009243:NAD; D000255:Adenosine Triphosphate; D007770:L-Lactate Dehydrogenase; D011770:Pyruvate Kinase; D000252:Calcium-Transporting ATPases; D016650:Fluorescein-5-isothiocyanate