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Biomedical subjects

C H Gray

Publications and source records attributed to C H Gray.

At least 37 records · Page 2Linked to original sources
PubMed1970

The oxidation products of crude mesobilirubinogen.

Bile pigment esters were separated by ascending t.l.c. Apparently pure pigments, obtained by ferric chloride oxidation of crude mesobilirubinogen, derived from commercial bilirubin by reduction with sodium amalgam, were shown to be complex mixtures. Successive chromatography of their dimethyl esters on silica gel in methyl acetate-methyl propionate-dichloromethane-carbon tetrachloride (1:1:1:1, by vol.), ethyl methyl ketone-1,2-dichloroethane (1:2, v/v) and benzene-ethanol (100:3, v/v) revealed two major blue pigments (verdins), six major violet pigments (violins) and a red pigment (rhodin) together with numerous minor components. i-Urobilin dimethyl ester, prepared from mesobilirubinogen by dehydrogenation with aqueous iodine, was resolved into three major and at least four minor components on silica gel-kieselguhr (3:1, w/w) in benzene-ethanol (25:2, v/v). The chemical nature of these pigments was investigated by oxidation, by visible and u.v. spectroscopy, by mass spectrometry and by n.m.r. spectrometry. The evidence suggests unusual rearrangement of bilirubin during reduction leading to the formation of IIIalpha and XIIIalpha isomers. Isomeric forms of mesobiliviolin IXalpha and of i-urobilin IXalpha may also be formed.

Bile Pigments↗
PubMed1967

Studies on haem alpha-methenyl oxygenase. Isomeric structure of formylbiliverdin, a possible precursor of biliverdin.

1. The enzyme from guinea-pig liver that degrades pyridine-haemochromogen into formylbiliverdin, a possible precursor of biliverdin, breaks the porphyrin ring exclusively at the alpha-methene bridge. The enzyme is therefore appropriately named haem alpha-methenyl oxygenase. 2. It is deduced that this enzyme plays an essential role in haemoglobin catabolism in vivo.

Animals↗