LIPOLYSIS OF FLUORESCEIN AND EOSIN ESTERS. KINETICS OF HYDROLYSIS.

摘要: Abstract A series of fluorescein and eosin esters have been prepared for use in the assay activity lipase acylase: diacetyl, dipropionyl, dichloropropionyl, dibutyryl, divaleryl, dicaproyl fluorescein, dibutyryl eosin. The were found to hydrolyze extremely slowly presence enzyme, even at pH's as high 10.0. rate hydrolysis by all enzymes except porcine pancreas was decrease order: acetyl > propionyl butyryl valeryl caproyl. With pancreas, divaleryl had a higher than ester. Steapsin, wheat germ lipase, well acylase, catalyze fluorescein. order is pancrease acylase steapsin lipase. kinetic thermodynamic constants ( K′ m , k 3 Δ E ∗ H′, F′, S′ ) various four different are reported. Sodium taurocholate increase chymotrypsin esters. Km, ΔH, ΔF, ΔS an k3 observed when this bile salt added reaction solutions. No effect on observed, thus indicating that probable lipolytic solubilization substrate.