Bile pigment formation <i>in vitro</i> from haematin and haem derivatives

Kench, J. E.

doi:10.1042/bj0560669

Cited by 26 publications

(10 citation statements)

References 21 publications

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“…The spectral results, in agreement with previous reports (Kench 1954), show that cytochrome c withstands the action of ascorbate or agents deriving from ascorbate. The spectral changes of hemoglobin and cytochrome c brought about by hydrazine hydrate are different in rate, hemoglobin reacting approximately 5 times faster.…”

Section: Discussionsupporting

confidence: 93%

“…Initially the light absorption decreases in the range 5W600 nm and increases above 600 nm, but then it decreases generally; during these changes carbon monoxide is evolved (Sjostrand 1952). Cytochrome c, however, resists coupled oxidation with ascorbic acid (Kench 1954). In the present experiments the spectral changes of cytochrome c and the evolution of carbon monoxide from this hemoprotein in the presence of some reductants have been followed. Carbon monoxide has been identified as a degradation product of ascorbic acid.…”

mentioning

confidence: 94%

“…The heme group of hemoglobin, myoglobin, catalase and plant peroxidase is degraded to bile pigments in an aerated solution of ascorbic acid or some other reductants (Sjostrand 1949, Sjostrand 1952, Kench 1954, Omura and Sat0 1964. Initially the light absorption decreases in the range 5W600 nm and increases above 600 nm, but then it decreases generally; during these changes carbon monoxide is evolved (Sjostrand 1952).…”

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confidence: 99%

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Carbon Monoxide as a Degradation Product of Cytochrome C and of Ascorbic Acid

Westman

1975

Acta Physiologica Scandinavica

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Cytochrome c has been incubated with 4 different reducing agents at 37 degrees C for 24 h at pH 7.0, and the spectral changes and the production of carbon monoxide have been followed. Only with hydrazine hydrate cytochrome c produced some carbon monoxide. Accidentally, carbon monoxide formation from ascorbic acid was found, amounting to about 0.1 mumol from 15 mumol of ascorbic acid in 24 h under the above conditions.

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Section: Discussionsupporting

confidence: 93%

mentioning

confidence: 94%

mentioning

confidence: 99%

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Carbon Monoxide as a Degradation Product of Cytochrome C and of Ascorbic Acid

Westman

1975

Acta Physiologica Scandinavica

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“…The failure to demonstrate conversion of oc-oxymesoporphyrin or ,B-oxymesoporphyrin into bile pigment in vivo is consistent with the known stability of porphyrins compared with haems in oxidation experiments in vitro (Kench, 1954). Administrationofa-oxymesoporphyrinwasfollowed by the disappearance of bilirubin from the bile and the rapid appearance of radioactivity; bilirubin reappeared in the bile only when radioactivity had decreased.…”

Section: V4supporting

confidence: 72%

Isotopic studies of the conversion of oxophlorins and their ferrihaems into bile pigments in the rat

Kondo

Nicholson

Jackson

et al. 1971

Biochemical Journal

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1. Tritiated oxymesoporphyrins and their ferrihaems were tested as possible intermediates in the catabolism of haemoglobin. The tritiated compounds were injected into rats with biliary fistulae and the incorporation of the isotope into bile, bile pigment, urine, faeces, liver, kidney and spleen was measured. 2. alpha-Oxymesoferrihaem was extensively converted into bile pigment and specifically to the expected mesobilirubin. 3. beta-Oxymesoferrihaem was poorly converted into bile pigment and was not converted into mesobiliverdin IXbeta. The latter was independently shown to be excreted rapidly in bile. 4. The free oxyporphyrins were also poor precursors of bile pigment, and alpha-oxymesoporphyrin competed with bilirubin for excretion by the liver. 5. By analogy with the results obtained with alpha-oxymesoferrihaem it is concluded that alpha-oxyprotoferrihaem is an intermediate in the catabolism of haemoglobin, undergoing further oxidation to bile pigment under the catalysis of an enzyme of definite specificity.

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“…One α-carbon in each pyrrole residue and each of the four bridge carbons was found to arise from the methyl carbon of glycine. Shemin and Kumin< 140 > subsequently showed that succinate was incorporated into heme without rearrangement. 4).…”

Section: B the Biogenesis Of Porphyrinsmentioning

confidence: 99%