By Michael B Bottorff, William E. Evans, Ingrid Hillebrand, Bodo Junge, Lutz Müller, Walter Puls, Delf D. Schmidt, Ernst Truscheit, Horst Will
Das Buch enthalt Kapitel uber: M. B. Bottorff, W. E. Evans, Memphis, TN, united states: Uberwachung der Medikament-KonzentrationE. Truscheit, I. Hillebrand, B. Junge, L. Muller, W. Puls, D. D. Schmidt, Wuppertal, FRG: Inhibitoren der mikrobiellen alpha-Glucosidase: Chemie, Biochemie und potentielle therapeutische AnwendungenH. Will, Berlin-Buch, GDR: Plasminogen-Aktivatoren: Molekuleigenschaften, biologische Zellfunktion und klinische Anwendung
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Extra resources for Drug Concentration Monitoring Microbial Alpha-Glucosidase Inhibitors Plasminogen Activators
At 100°C. The hydrolysate was applied to a Dowex® 50 WX4, H+, 1 x 20 cm column and washed with 200 ml H 2 0. Desorption was started with 0,05 N HCI. Fractions of 2 m1 were taken. Aliquots were tested for inhibitory activity and total carbohydrate content (anthrone reaction, E620 ) E. Truscheit et al. 30 show that higher molecular components are eluted first, and that with marked amylase inhibition only slight inhibition of sucrase occurs. The inhibitors eluted towards the end of the separation process show a completely reversed specificity of inhibition.
Nd that of man, rabbit, and chicken is not inhibited. (X-Amylase from human saliva and urine is also not inhibited. No inhibitory activity has been detected against (X- and ~-amylase of plant origin or against Rhizopus niveus glucoamylase. A peptide inhibitor (AI-B) of remarkable specificity for pancreatic (X-amylases was isolated by Harada et al. 126) from cultures of Streptomyces viridosporus. 7. In contrast to pancreatic (X-amylase, salivary (X-amylase, bacterial (X-amylase, glucoamylase, and malt-~-amylase are only weakly inhibited.
Ltd. are - as has recently been described 48,49) - built up according to the same structural principle as the individual members of the homologous acarbose series. For example, various products obtained by degradation of higher molecular inhibitors by p-amylase contain the acarviosine residue as the essential component responsible for the inhibitory activity of the compounds and are identical to homologues of acarbose described previously. , 1975) (32) (K. 49) 34 (M. , 1979)(51) (K. , 1980) (52,53) 35 (s.