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Biomedical subjects

C Rimington

Publications and source records attributed to C Rimington.

At least 55 records · Page 3Linked to original sources
PubMed1970

Identification of the acrylate porphyrin S-411 from meconium.

A new porphyrin isolated from calf and foal meconium has been characterized as a tris-(2-carboxyethyl)-mono-(2-carboxyvinyl)-tetramethyl porphin, that is as an analogue of coproporphyrin in which one propionate group has been replaced by an acrylate group. The porphyrin is mainly a type III isomer and its possible significance in haem biosynthesis is discussed.

Acrylates↗
PubMed1968

Royal malady.

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History, 17th Century↗
PubMed1967

Partition of porphyrins between cyclohexanone and aqueous sodium acetate as a function of pH. Determination of uroporphyrin and of hydrophilic porphyrin conjugates.

1. The partition of uroporphyrins I and III, coproporphyrins I and III, haematoporphyrin IX, porphyrin c and a hydrophilic porphyrin-peptide fraction from variegate-porphyria faeces has been studied in systems of equal volumes of cyclohexanone and sodium acetate buffers of varying pH and concentration. 2. The concentration of acetate in the aqueous phase has little effect on the partition of porphyrin c, but markedly influences that of uroporphyrin. At 50% acetate saturation and pH4.5, only 5% enters the cyclohexanone phase whereas 60% of porphyrin c is extracted under similar conditions. 3. This circumstance forms the basis of a method for the determination of hydrophilic porphyrin-peptides in variegate-porphyria urine. Its reliability has been checked in model experiments. 4. At pH1.5 and an aqueous phase half-saturated with sodium acetate, an equal volume of cyclohexanone removes 95-97% of uroporphyrin and about 55% of porphyrin c. Uroporphyrin may therefore be determined as a second step in the method. 5. For the routine determination of uroporphyrin in systems free from other hydrophilic porphyrins, cyclohexanone extraction may be performed at any pH in the range 1.0-3.0.

Journal Article↗
PubMed1965

Purification and properties of coproporphyrinogenase.

1. Coproporphyrinogenase has been prepared from rat-liver mitochondria and its properties have been studied. The isoelectric point was found to be around pH5.0 and the molecular weight to be 80000+/-8000. The pH optimum of the enzymic reaction was 7.4 and the apparent K(m) was of the order 0.03mm. The enzyme was destroyed by boiling and irreversible inactivation occurred below pH3.5. It could be stored at -10 degrees without loss of activity. The enzyme acts specifically on coproporphyrinogen III and does not form protoporphyrinogen from trans-2,4-diacrylicdeuteroporphyrin or its porphyrinogen. It was unaffected by prolonged dialysis and no cofactor requirement could be demonstrated. 2. Column chromatography of a partially purified enzyme preparation on Sephadex G-200 was found to be an improved method of purification, which gave a coproporphyrinogenase 58-fold purified. The purified enzyme was studied electrophoretically but no evidence was obtained to suggest that more than one enzyme was involved in the reaction. 3. The action was studied of various compounds added to the system. The presence of monothiol groups in the enzyme system was indicated, whereas vicinal dithiol groups were not involved in the reaction. Metal-chelating agents did not inhibit the reaction and no requirement for the presence of any essential metal has been found. All attempts to demonstrate the presence of a prosthetic group, in particular flavines, failed. Neither pyridoxal phosphate nor ATP was involved in the reaction, nor was a mitochondrial electron-transport chain required for the activity of the enzyme. Some circumstantial evidence was obtained to suggest that cis-2,4-diacrylicdeuteroporphyrin is an intermediate in the reaction.

Animals↗