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The paper deals with the activity of peptidohydrolases splitting hemoglobin, casein and benzoylarginine-p-nitroanilide (BAPNA) in the ontogenesis of Drosophila mutant white apricot (wa). The enzymic activity is high in the intestine tissue at the larval stage, but it does not manifest itself at the pupal stage that may be due to inactivation of the studied enzymes by inhibitors found in extracts of the pupal tissues. The imaginal period of development is characterized by a low level of the peptidohydrolase activity in females and its absence in males in whose tissues there is a high content of inhibitors. The peptidohydrolase activity in extracts of larval tissues is established to be dependent completely on the enzyme being in the intestinal wall. Incomplete purification of this peptidohydrolase and its inhibitor is performed by means of ion-exchange chromatography on DEAE-cellulose. Some of their physicochemical properties are investigated.
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The recovery measurements in rat tissues performed via i.p. injected radioactive digoxin derivates (3H-digoxin, 125J-digoxin derivative) showed that approximately 50% of the total glycoside content will be extracted. Thus, an addition of digoxin standards to drug-free tissues may lead to false negative determinations. By comparison of the radioactivity before and after extraction the following results were obtained: Recovery from tissues 3H-digoxin 50% 125J-digoxin 40% from serum 3H-digoxin 60% added to drug free tissue homogenates 3H-digoxin 85% After i.p. application of 15 mg/kg of beta-methyldigoxin to BD9 (Berlin)-rats the resulting tissue concentrations were extracted by Amberlite XAD-2. beta-Methyldigoxin and its metabolites digoxin and digoxinbisdigitoxide could be separated and distinguished from artifacts by fluorescence detection on HPTLC-plates with a detection limit of 60 ng/spot. Concentration determined by radioimmunoassay are in satisfactory agreement with HPTLC results.
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