VANILLINSÄURE ALS ENDPRODUKT DES ABBAUES VON ADRENALIN UND NORADRENALIN

1964 ◽  
Vol 45 (4) ◽  
pp. 641-646 ◽  
Author(s):  
Wilhelm Dirscherl ◽  
Betty Brisse

ABSTRACT Incubation of homogenates of rat liver or human liver with D,L-3-methoxy-4-hydroxy-mandelic acid yielded 3 diazopositive compounds. In addition to the starting material, vanillic acid could be isolated by means of column chromatography. It was identified by the shape of its crystals, micro melting point, mixed melting point, UV- and IR-spectra, and paper chromatography in 3 different solvent systems. The third substance has not yet been identified. Since acid hydrolysis does not result in any cleavage a conjugate can be ruled out. The yield of vanillic acid was about 12 per cent with rat liver, 3 per cent with post mortem liver and 7-8 per cent with liver obtained at operation. Vanillic acid is not further metabolized by liver homogenates and can also be considered as the final metabolite of adrenaline and noradrenaline in the human liver.

1964 ◽  
Vol 47 (1) ◽  
pp. 69-75 ◽  
Author(s):  
Helmut Thomas ◽  
Wilhelm Dirscherl

ABSTRACT After incubation of 3-methoxy-4-hydroxy-mandelic acid, a metabolite of adrenaline and noradrenaline, with rat liver slices and slices of human liver obtained at post mortem, in addition to vanillic acid one intermediary product was detected by paper chromatography. In the system benzene-propionic acid-water (2:2:1) this showed the same RF-value as 3-methoxy-4-hydroxy-benzaldehyde (vanillin). In the deproteinized incubation medium the substance was precipitated as 2,4-dinitrophenylhydrazone, which after purification and recrystallisation was identified by melting point, absorption spectrum between 220 and 500 mμ, and IR-spectrum as 2,4-dinitrophenylhydrazone of vanillin.


1962 ◽  
Vol 39 (3) ◽  
pp. 385-394 ◽  
Author(s):  
Wilhelm Dirscherl ◽  
Helmut Thomas ◽  
Herbert Schriefers

ABSTRACT In rat livers perfused with 3-methoxy-4-hydroxy-mandelic acid, formerly believed to be the endproduct of the metabolism of adrenaline and noradrenaline, three metabolites were detected by paper chromatography. After further purification by column chromatography, one of these substances was identified by melting point, shape of crystals, UV- and IR-spectra as vanillic acid. Perfusion with vanillic acid yielded only one metabolite in very small quantities. Because of its properties it is assumed to be a conjugate of vanillic acid. Hence vanillic acid, isolated in 1959 from human urine by Dirscherl & Schmidtmann, is the actual endproduct of the metabolism of adrenaline and noradrenaline.


1963 ◽  
Vol 44 (1) ◽  
pp. 101-106 ◽  
Author(s):  
Wilhelm Dirscherl ◽  
Helmut Thomas

ABSTRACT Perfusion of rat liver with vanillic acid yielded only one metabolite. In paper chromatography with three different solvent systems, the substance showed the same RF-values as vanillyolglycine (3-methoxy-4-hydroxyhippuric acid) and in mixed chromatograms there was only one single spot. After separation by column chromatography, the UV- and IRspectra of the reaction product were identical with those of 3-methoxy4-hydroxy-hippuric acid. During the perfusion experiment, the kinetics of the conjugation were investigated.


1983 ◽  
Vol 209 (3) ◽  
pp. 831-836 ◽  
Author(s):  
L Stowell ◽  
J Mørland

1. With two different methods for assaying the tryptophan oxygenase activity in rat liver homogenates, the effects of some methodological factors on the activity of the enzyme were studied. 2. In fed, but not in starved, rats a compound(s) absorbing at 365 nm, interfering with the reading of kynurenine absorbance, disappeared gradually during incubation. 3. A correction for this tryptophan-independent reaction was necessary in order to determine correct tryptophan oxygenase activity. 4. Blood remaining in liver tissue post mortem can serve as a source of cofactor haem for tryptophan oxygenase, causing spuriously high values for the activity of the holoenzyme form of tryptophan oxygenase. 5. A rapid and progressive activation of tryptophan oxygenase post mortem occurs in undisrupted liver tissue, and this activation is temperature-dependent.


1985 ◽  
Vol 232 (2) ◽  
pp. 459-466 ◽  
Author(s):  
H Iwahashi ◽  
A Ikeda ◽  
R Kido

Examination of the subcellular distribution of retinoic acid 5,6-epoxidase activity in rat liver and human liver homogenates showed that there is a prominent peak of activity in a high-density fraction. A corresponding peak was also detected in rat blood and human blood. Retinoic acid 5,6-epoxidation was catalysed by human blood cells but not by human plasma, and purified human haemoglobin also catalysed the epoxidation of retinoic acid to 5,6-epoxyretinoic acid. These results suggest that retinoic acid 5,6-epoxidase activity in human liver and rat liver homogenates is partially due to the presence of residual blood cells, and particularly haemoglobin, in the homogenates. In the retinoic acid 5,6-epoxidation catalysed by human haemoglobin, molecular O2 was required and its reaction was stimulated by Triton X-100. Boiling of haemoglobin solution resulted in an 94% decrease in the activity. NADPH (1 mM) and NADH (1 mM) completely [2-mercaptoethanol (5 mM) almost completely] inhibited the 5,6-epoxidation catalysed by haemoglobin, but catalase, superoxide dismutase and mannitol showed no inhibitory effect. CN- ion (100 mM) inhibited the reaction, but N3- ion (100 mM) did not.


2006 ◽  
Vol 44 (01) ◽  
Author(s):  
T Mansuroglu ◽  
J Dudas ◽  
B Saile ◽  
D Batusic ◽  
G Ramadori

1954 ◽  
Vol 206 (1) ◽  
pp. 471-481 ◽  
Author(s):  
Ivan D. Frantz ◽  
Nancy L.R. Bucher ◽  
Henny S. Schneider ◽  
Naomi H. McGovern ◽  
Ruth Kingston

1957 ◽  
Vol 225 (2) ◽  
pp. 735-744
Author(s):  
Henry Kamin ◽  
Mildred A. Koon ◽  
Philip Handler
Keyword(s):  

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