Substrate specificity of lentil seedling amine oxidase
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چکیده
منابع مشابه
Conformational lock and dissociative thermal inactivation of lentil seedling amine oxidase.
The kinetics of thermal inactivation of copper-containing amine oxidase from lentil seedlings were studied in a 100 mM potassium phosphate buffer, pH 7, using putrescine as the substrate. The temperature range was between 47-60 degrees C. The thermal inactivation curves were not linear at 52 and 57 degrees C; three linear phases were shown. The first phase gave some information about the number...
متن کاملTransient kinetics of copper-containing lentil (Lens culinaris) seedling amine oxidase.
The reaction between lentil (Lens culinaris) seedling amine oxidase and its chromogenic substrate, p-dimethylaminomethylbenzylamine, has been studied by the stopped-flow technique. Upon being mixed with substrate in the absence of oxygen, the enzyme is bleached in a complex kinetic process. A yellow intermediate absorbing at 464 nm and the first product (aldehyde) are formed in subsequent steps...
متن کاملThermal dissection of lentil seedling amine oxidase domains by differential scanning calorimetry.
The relationships between the structural and energetic domains of lentil seedling amine oxidase (LSAO) were investigated using modifiers that target the active site and the carbohydrate moiety of the enzyme. An irreversible inhibitor, aminoguanidine, specifically modified the active site of the lentil enzyme, whereas sodium metaperiodate cleaves carbohydrate moieties covalently bound to the nat...
متن کاملInhibitor Specificity of Amine Oxidase
In their studies of the oxidation of adrenalin and other amines by amine oxidase preparations, Blaschko, Richter, and Schlossmann (1) found that l-ephedrine, triethylamine, triisoamylamine, and dl-1-hydroxy-2-hydrindeneamine are not only not oxidized, but inhibit the action of the enzyme upon isoamylamine. The conclusion was drawn that this inhibition was of the competitive type, because some d...
متن کاملSubstrate specificity of amine oxidases.
DuBois, K. P., Albaum, H. G. & Potter, V. R. (1943). J. biol. Chem. 147, 699. Green, H. N. (1943). Lancet, 2, 147. Green, H. N. & Stoner, H. B. (1944). Brit. J. exp. Path. 25, 150. Kal¢kar, H. M. (1943). J. biol. Chem. 148, 127. Kolthoff, I. M. (1932). Saure-Ba8en Indicatoren. Berlin: Springer. Krebs, H. A. & Henseleit, K. (1932). Ho.ppe-Seyl. Z. 210, 33.' Lyubimova, M. N. & Pevsner, D. (1941)....
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ژورنال
عنوان ژورنال: IUBMB Life
سال: 1996
ISSN: 1521-6543
DOI: 10.1080/15216549600201223