Purification and properties of human erythrocyte uroporphyrinogen decarboxylase

immunological demonstration of the enzyme defect in porphyria cutanea tarda.

S. Sassa, H. de Verneuil, Karl Anderson, A. Kappas

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

The first complete purification of UROD from human erythrocytes and the characterization of the purified enzyme were described. A single enzyme protein catalyzes the four successive sequential decarboxylations of uroporphyrinogen to yield coproporphyrinogen. The enzyme activity is not directly inhibited by iron; however, it is subject to inhibition in liver cells by a number of chemicals, including environmental pollutants such as dioxin. Studies of erythrocyte UROD in PCT patients indicate that the group of patients now defined as having sporadic PCT may represent two different populations; i.e., those who have normal UROD, and those who have decreased UROD in erythrocytes. Genetic heterogeneity of the UROD defect in PCT is also indicated by the identification of both CRM(-) and CRM(+) mutations in this disorder.

Original languageEnglish
Pages (from-to)65-75
Number of pages11
JournalTransactions of the Association of American Physicians
Volume96
StatePublished - 1983
Externally publishedYes

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Uroporphyrinogen Decarboxylase
Porphyria Cutanea Tarda
Erythrocytes
Coproporphyrinogens
Enzymes
Uroporphyrinogens
Environmental Pollutants
Decarboxylation
Dioxins
Genetic Heterogeneity
Iron
Cell Count
Mutation
Liver
Population
Proteins

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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title = "Purification and properties of human erythrocyte uroporphyrinogen decarboxylase: immunological demonstration of the enzyme defect in porphyria cutanea tarda.",
abstract = "The first complete purification of UROD from human erythrocytes and the characterization of the purified enzyme were described. A single enzyme protein catalyzes the four successive sequential decarboxylations of uroporphyrinogen to yield coproporphyrinogen. The enzyme activity is not directly inhibited by iron; however, it is subject to inhibition in liver cells by a number of chemicals, including environmental pollutants such as dioxin. Studies of erythrocyte UROD in PCT patients indicate that the group of patients now defined as having sporadic PCT may represent two different populations; i.e., those who have normal UROD, and those who have decreased UROD in erythrocytes. Genetic heterogeneity of the UROD defect in PCT is also indicated by the identification of both CRM(-) and CRM(+) mutations in this disorder.",
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T1 - Purification and properties of human erythrocyte uroporphyrinogen decarboxylase

T2 - immunological demonstration of the enzyme defect in porphyria cutanea tarda.

AU - Sassa, S.

AU - de Verneuil, H.

AU - Anderson, Karl

AU - Kappas, A.

PY - 1983

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AB - The first complete purification of UROD from human erythrocytes and the characterization of the purified enzyme were described. A single enzyme protein catalyzes the four successive sequential decarboxylations of uroporphyrinogen to yield coproporphyrinogen. The enzyme activity is not directly inhibited by iron; however, it is subject to inhibition in liver cells by a number of chemicals, including environmental pollutants such as dioxin. Studies of erythrocyte UROD in PCT patients indicate that the group of patients now defined as having sporadic PCT may represent two different populations; i.e., those who have normal UROD, and those who have decreased UROD in erythrocytes. Genetic heterogeneity of the UROD defect in PCT is also indicated by the identification of both CRM(-) and CRM(+) mutations in this disorder.

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