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Erythropoietic protoporphyria and lead intoxication: the molecular basis for difference in cutaneous photosensitivity. II. Different binding of erythrocyte protoporphyrin to hemoglobin.
J Clin Invest. 1975 Dec; 56(6):1528-35.JCI

Abstract

Acidic solvents extract the same porphyrin-protoporphyrin-from the erythrocytes of patients with either erythropoietic protoporphyria or lead intoxication. However, extractable protoporphyrin disappears rapidly, both in vivo and in vitro, from erythrocytes in erythropoietic protoporphyria but slowly, if at all, in lead intoxication. Consistent with these observations, fluorescence spectroscopy revealed that the intracellular state of the erythrocyte protoporphyrin is different in the two diseases. Spectrofluorometric measurements coupled with fractionations and biochemical syntheses showed that in erythropoietic protoporphyria the protoporphyrin is bound as the free base to hemoglobin molecules at sites other than the heme binding sites. In lead intoxication the fluorescent porphyrin is also bound to hemoglobin but is present as zinc protoporphyrin. The data suggest that the zinc protoporphyrin is bound at heme binding sites. Acidic extraction solvents remove the chelated zinc, but zinc protoporphyrin may be extracted intact from erythrocytes with acetone, ethanol, or the detergent Ammonyx-LO.

Authors

No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

1202083

Citation

Lamola, A A., et al. "Erythropoietic Protoporphyria and Lead Intoxication: the Molecular Basis for Difference in Cutaneous Photosensitivity. II. Different Binding of Erythrocyte Protoporphyrin to Hemoglobin." The Journal of Clinical Investigation, vol. 56, no. 6, 1975, pp. 1528-35.
Lamola AA, Piomelli S, Poh-Fitzpatrick MG, et al. Erythropoietic protoporphyria and lead intoxication: the molecular basis for difference in cutaneous photosensitivity. II. Different binding of erythrocyte protoporphyrin to hemoglobin. J Clin Invest. 1975;56(6):1528-35.
Lamola, A. A., Piomelli, S., Poh-Fitzpatrick, M. G., Yamane, T., & Harber, L. C. (1975). Erythropoietic protoporphyria and lead intoxication: the molecular basis for difference in cutaneous photosensitivity. II. Different binding of erythrocyte protoporphyrin to hemoglobin. The Journal of Clinical Investigation, 56(6), 1528-35.
Lamola AA, et al. Erythropoietic Protoporphyria and Lead Intoxication: the Molecular Basis for Difference in Cutaneous Photosensitivity. II. Different Binding of Erythrocyte Protoporphyrin to Hemoglobin. J Clin Invest. 1975;56(6):1528-35. PubMed PMID: 1202083.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Erythropoietic protoporphyria and lead intoxication: the molecular basis for difference in cutaneous photosensitivity. II. Different binding of erythrocyte protoporphyrin to hemoglobin. AU - Lamola,A A, AU - Piomelli,S, AU - Poh-Fitzpatrick,M G, AU - Yamane,T, AU - Harber,L C, PY - 1975/12/1/pubmed PY - 1975/12/1/medline PY - 1975/12/1/entrez SP - 1528 EP - 35 JF - The Journal of clinical investigation JO - J Clin Invest VL - 56 IS - 6 N2 - Acidic solvents extract the same porphyrin-protoporphyrin-from the erythrocytes of patients with either erythropoietic protoporphyria or lead intoxication. However, extractable protoporphyrin disappears rapidly, both in vivo and in vitro, from erythrocytes in erythropoietic protoporphyria but slowly, if at all, in lead intoxication. Consistent with these observations, fluorescence spectroscopy revealed that the intracellular state of the erythrocyte protoporphyrin is different in the two diseases. Spectrofluorometric measurements coupled with fractionations and biochemical syntheses showed that in erythropoietic protoporphyria the protoporphyrin is bound as the free base to hemoglobin molecules at sites other than the heme binding sites. In lead intoxication the fluorescent porphyrin is also bound to hemoglobin but is present as zinc protoporphyrin. The data suggest that the zinc protoporphyrin is bound at heme binding sites. Acidic extraction solvents remove the chelated zinc, but zinc protoporphyrin may be extracted intact from erythrocytes with acetone, ethanol, or the detergent Ammonyx-LO. SN - 0021-9738 UR - https://www.unboundmedicine.com/medline/citation/1202083/Erythropoietic_protoporphyria_and_lead_intoxication:_the_molecular_basis_for_difference_in_cutaneous_photosensitivity__II__Different_binding_of_erythrocyte_protoporphyrin_to_hemoglobin_ L2 - https://doi.org/10.1172/JCI108234 DB - PRIME DP - Unbound Medicine ER -