Results 1 to 10 of about 3,315 (223)
Effects of Chemical Structures Interacting with Amine Oxidases on Glucose, Lipid and Hydrogen Peroxide Handling by Human Adipocytes [PDF]
Molecules, 2022 Benzylamine is a natural molecule present in food and edible plants, capable of activating hexose uptake and inhibiting lipolysis in human fat cells.
Christian Carpéné +6 more
doaj +2 more sources
Unprecedented lysyloxidase activity of Pichia pastoris benzylamine oxidase [PDF]
FEBS Letters, 1988 Benzylamine oxidase (EC 1.4.3.6) from the yeast Pichia pastoris is a 106 kDa quinoprotein containing one copper atom per molecule. It has a broad substrate specificity ranging from butylamine to peptidyl lysine in collagen and elastin. The kinetic data obtained using lysine‐containing model peptides as substrates indicate an astonishing similarity to ...
Sigmund S. Tur, Konrad Lerch
openalex +4 more sources
Benzylamine oxidase from brain microvessels [PDF]
FEBS Letters, 1983 Copper‐containing benzylamine oxidase with a specific activity of 200 units was isolated from bovine brain microvessels. It was shown that the content of the enzyme in microvessels was significantly higher as compared with large blood vessels such as heart aorta. Some physico‐chemical properties of the enzyme were determined.
Z.B. Mehrabian, R.M. Nalbandyan
openalex +3 more sources
Active-Site Titration of Pig-Plasma Benzylamine Oxidase [PDF]
European Journal of Biochemistry, 1978 1. Titration of benzylamine oxidase with benzylamine under anaerobic conditions shows that full reduction of the enzymic 470-nm chromophore is obtained on the addition of one mole of substrate per mole of enzyme. Concomitantly, one mole of benzaldehyde per mole of enzyme is produced. 2.
Anders Lindström, Gösta Pettersson
openalex +3 more sources
The Kinetics of Reoxidation of Reduced Benzylamine Oxidase [PDF]
European Journal of Biochemistry, 1977 The mechanism of reoxidation of reduced benzylamine oxidase has been investigated at different pH between 6 and 10 by steady‐state and transient‐state kinetic methods. The reoxidation process involves minimally a second‐order interaction between reduced enzyme and oxygen leading to the formation of a spectrally modified enzyme intermediate, and a ...
Bengt A. Olsson +2 more
openalex +3 more sources
Benzylamine oxidase : an enzyme in search of a function. [PDF]
, 1980 Imperial Users ...
Rachel Lewinsohn
core +4 more sources
Active-sitve titration of pig plasma benzylamine oxidase with phenylhydrazine [PDF]
Biochemical Journal, 1975 Pig plasma benzylamine oxidase is a protein containing cupric copper and pyridoxal phosphate. The pyridoxal phosphate is stably linked to the enzyme. Discrepancies in the numbers of active sites per molecule of enzyme are reported in the literature.
F. Buffoni, G. Ignesti
openalex +4 more sources
Effect of pH on the Transient Reduction of Pig-Plasma Benzylamine Oxidase by Benzylamine Derivatives [PDF]
European Journal of Biochemistry, 1976 1. The transient kinetics of reduction of the 470-nm absorption band in benzylamine oxidase by substrate at different pH values between 6 and 10 have been studied by stopped-flow techniques, and substituent effects on kinetic parameters for the reduction process have been examined using a series of ring-substituted benzylamine derivatives as the ...
Anders Lindström +3 more
openalex +4 more sources
Steady‐State Kinetic Studies on Benzylamine Oxidase from Pig Plasma [PDF]
European Journal of Biochemistry, 1981 Steady‐state kinetic studies on the enzyme benzylamine oxidase from pig plasma are described. Eadie‐Hofstee plots with benzylamine as the varying substrate are non‐linear; examination of this data indicates that the observed effects are probably due to the amine substrate participating in at least two reactions with enzyme. Ammonia and imidazole modify
I D Kelly +5 more
openalex +3 more sources
Methylxanthines Inhibit Primary Amine Oxidase and Monoamine Oxidase Activities of Human Adipose Tissue [PDF]
Medicines, 2020 Background: Methylxanthines including caffeine and theobromine are widely consumed compounds and were recently shown to interact with bovine copper-containing amine oxidase.
Wiem Haj Ahmed +8 more
doaj +3 more sources