Determination of the anxiolytic agent 8-chloro-6-(2-chlorophenyl)-4H-imidazo-[1,5-alpha] [1,4]-benzodiazepine-3-carboxamide in whole blood, plasma or urine by high-performance liquid chromatography.
A rapid, sensitive and specific high-performance liquid chromatographic (HPLC) assay was developed for the determination of 8-chloro-6-(2-chlorophenyl)-4H-imidazo-[1,5-alpha]-[1,4]-benzodiazepine-3-carboxamide [I] and its 4-hydroxy metabolite, 8-chloro-6-(2-chlorophenyl)-4-hydroxy-4H-imidazo-[1,5-alpha] [1,4]-benzodiazepine-3-carboxamide [II] in whole blood, plasma or urine. The assay for both compounds involves extraction into diethyl ether-methylene chloride (70:30) from blood, plasma, or urine buffered to pH 9.0. The overall recoveries of [I] and [II] are 92.0 +/- 5.4% (S.D.) and 90.3 +/- 4.9% (S.D.), respectively. The sensitivity limit of detection is 50 ng/ml of blood, plasma, or urine using a UV detector at 254 nm. The HPLC assay was used to monitor the blood concentration-time fall-off profiles, and urinary excretion profiles in the dog following single 1 mg/kg intravenous and 5 mg/kg oral doses, and following multiple oral doses of 100 mg/kg/day of compound [I].
Quinazolines and 1,4‐benzodiazepines. LXXXV syntheses of 3‐substituted lmidazo[1,5‐a] [1,4]benzodiazepines
1,4-Benzodiazepines having a leaving group in the 2-position were condensed with carbanions of 1,3-dicarbonyl compounds. The products obtained were converted to the title compounds by a sequence of steps involving hydrolytic decarboxylation, nitrosation, catalytic hydrogenation and condensation with an orthoester or an amide acetal. 
 
 
 
Oxidative condensation of the enediamine 12 with a variety of aldehydes also led to imidazo-benzodiazepines with various substituents in the 1-position.
Glycogen phosphorylase in lobster hepatopancreas: action of proteases on the enzyme
Abstract 1. 1. In lobster hepatopancreas, extracellular protreases cause the inactivation of glycogen phosphorylase. 2. 2. The proteolysis of glycogen phosphorylase purified from rabbit muscle by these proteases has been shown by SDS-polyacrylamide gel electrophoresis. 3. 3. A cell isolation technique has allowed us to remove proteases of extracellular digestion and to measure glycogen phosphorylase activity in lobster hepatopancreas. 4. 4. The glycogen phosphorylase activity seems to be mainly associated with R cells while it could not be detected in B cells.