Combination of planar chromatography with matrix-assisted laser desorption/ionization mass spectrometry for the analysis of biologically active compounds

Author: D. I. Zhilyaev ; V. G. Zaikin ; R. S. Borisov ; C. A. Esparsa Sandoval ; N. Yu. Polovkov

MALDI mass spectra of 33 pharmacol. substances recorded from standard metal targets using four different matrixes (HABA, DHB, IAA and AT) have been obtained for the first time.They revealed only peaks for ions [M + H]⁺, [M + Na]⁺, and [M + K]⁺ with different intensities.It has been shown that MALDI spectra of the compounds can be obtained as a result of the desorption/ionization of analytes from spots on thin-layer chromatogram (TLC) (silica stationary phase) in the presence of the same tested matrixes.It has been found that graphite can be efficiently used as a matrix in combination of TLC with MALDI mass spectrometry, as it eliminates the danger of the broadening of spots on TLC plates in the treatment with matrix solution and reduces the time of sample preparation

01 Oct 2011·Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology

Erratum to “Catalytic and inhibitor binding properties of zebrafish monoamine oxidase (zMAO): Comparisons with human MAO A and MAO B” [Comp. Biochem. Physiol. Part B 159 (2011) 78-83]

Author: Betül Kacar Arslan ; Milagros Aldeco ; Dale E. Edmondson

On page 80, the first citation on the right side contained an error; the corrected citation is given.On page 81, the footnote to Table 2 contained a citation error; the corrected citation is given.On page 83, the fifth reference from the end contained an error; the corrected reference is given.

01 Jun 2011·Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular BiologyQ3 · BIOLOGY

Catalytic and inhibitor binding properties of zebrafish monoamine oxidase (zMAO): Comparisons with human MAO A and MAO B

Q3 · BIOLOGY

Article

Author: Arslan, Betuel Kacar ; Edmondson, Dale E. ; Aldeco, Milagros

A comparative investigation of substrate specificity and inhibitor binding properties of recombinant zebrafish (Danio rerio) monoamine oxidase (zMAO) with those of recombinant human monoamine oxidases A and B (hMAO A and hMAO B) is presented. zMAO oxidizes the neurotransmitter amines (serotonin, dopamine and tyramine) with k(cat) values that exceed those of hMAO A or of hMAO B. The enzyme is competitively inhibited by hMAO A selective reversible inhibitors with the exception of d-amphetamine where uncompetitive inhibition is exhibited. The enzyme is unreactive with most MAO B-specific reversible inhibitors with the exception of chlorostyrylcaffeine. zMAO catalyzes the oxidation of para-substituted benzylamine analogs exhibiting (D)k(cat) and (D)(k(cat)/K(m)) values ranging from 2 to 8. Structure-activity correlations show a dependence of log k(cat) with the electronic factor σ(p) with a ρ value of +1.55±0.34; a value close to that for hMAO A but not with MAO B. zMAO differs from hMAO A or hMAO B in benzylamine analog binding correlations where an electronic effect (ρ=+1.29±0.31) is observed. These data demonstrate zMAO exhibits functional properties similar to hMAO A as well as exhibits its own unique behavior. These results should be useful for studies of MAO function in zebrafish models of human disease states.

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