Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humans

Autores
Parera, V.E.; Stella, A.M.; De Xifra, E.A.W.; Fukuda, H.; Del C. Batlle, A.M.
Año de publicación
1980
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
1. 1. Studies on porphyrin biosynthesis from exogenus ALA, at various time intervals as well as direct enzyme measurements (aminolevulimc acid dehydratase (ALA-D); porphobilinogenase (PBG ase) and deaminase were carried out in hemolysates of human erythrocytes from healthy controls and patients with lead poisoning (Pb), acute intermittent porphyria (AIP), porphyria cutanea tarda (PCT), erythropoietic protoporphyria (EPP), variegate porphyria (VP) and congenital erythropoietic porphyria (CEP). 2. 2. Inhibited ALA-D in Pb, reduced PBGase and deaminase in AIP, lower uroporphyrinogen decarboxylase in PCT, and diminished isomerase in CEP, were confirmed. In addition, ALA-D was found, reduced in AIP, unchanged in PCT and increased in EPP, VP and CEP. PBGase and deaminase were, on the other hand, increased in Pb and PCT, unchanged in VP and diminished in EPP and CEP. 3. 3. Total porphyrin biosynthesis is a function of time; compared to normals, is lower in CEP and AIP, but higher in PCT. 4. 4. The porphyrin profile changes along the time; uroporphyrin increases at longer intervals while that of coproporphyrin concomitantly diminished. A significance enhancement of octacarboxylic porphyrins was observed during the entire duration of the incubation in PCT hemolysates. In CEP the main porphyrin was always uroporphyrin I. 5. 5. Studies on both total porphyrins formed and their distribution were performed in hemolysates from cases of non-hereditary and hereditary PCT and AIP, before and after therapy. © 1980.
Fil:Parera, V.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Fukuda, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fuente
Int. J. Biochem. 1980;12(5-6):947-953
Materia
ammonia lyase
Ammonia Lyases
porphobilinogen deaminase
porphobilinogen synthase
porphyrin
acute disease
article
biosynthesis
blood
enzymology
erythrocyte
human
newborn
porphyria
reference value
skin disease
Acute Disease
Ammonia-Lyases
Erythrocytes
Human
Hydroxymethylbilane Synthase
Infant, Newborn
Porphobilinogen Synthase
Porphyria
Porphyrins
Reference Values
Skin Diseases
Support, Non-U.S. Gov't
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/2.5/ar
Repositorio
Biblioteca Digital (UBA-FCEN)
Institución
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
OAI Identificador
paperaa:paper_0020711X_v12_n5-6_p947_Parera

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oai_identifier_str paperaa:paper_0020711X_v12_n5-6_p947_Parera
network_acronym_str BDUBAFCEN
repository_id_str 1896
network_name_str Biblioteca Digital (UBA-FCEN)
spelling Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humansParera, V.E.Stella, A.M.De Xifra, E.A.W.Fukuda, H.Del C. Batlle, A.M.ammonia lyaseAmmonia Lyasesporphobilinogen deaminaseporphobilinogen synthaseporphyrinacute diseasearticlebiosynthesisbloodenzymologyerythrocytehumannewbornporphyriareference valueskin diseaseAcute DiseaseAmmonia-LyasesErythrocytesHumanHydroxymethylbilane SynthaseInfant, NewbornPorphobilinogen SynthasePorphyriaPorphyrinsReference ValuesSkin DiseasesSupport, Non-U.S. Gov't1. 1. Studies on porphyrin biosynthesis from exogenus ALA, at various time intervals as well as direct enzyme measurements (aminolevulimc acid dehydratase (ALA-D); porphobilinogenase (PBG ase) and deaminase were carried out in hemolysates of human erythrocytes from healthy controls and patients with lead poisoning (Pb), acute intermittent porphyria (AIP), porphyria cutanea tarda (PCT), erythropoietic protoporphyria (EPP), variegate porphyria (VP) and congenital erythropoietic porphyria (CEP). 2. 2. Inhibited ALA-D in Pb, reduced PBGase and deaminase in AIP, lower uroporphyrinogen decarboxylase in PCT, and diminished isomerase in CEP, were confirmed. In addition, ALA-D was found, reduced in AIP, unchanged in PCT and increased in EPP, VP and CEP. PBGase and deaminase were, on the other hand, increased in Pb and PCT, unchanged in VP and diminished in EPP and CEP. 3. 3. Total porphyrin biosynthesis is a function of time; compared to normals, is lower in CEP and AIP, but higher in PCT. 4. 4. The porphyrin profile changes along the time; uroporphyrin increases at longer intervals while that of coproporphyrin concomitantly diminished. A significance enhancement of octacarboxylic porphyrins was observed during the entire duration of the incubation in PCT hemolysates. In CEP the main porphyrin was always uroporphyrin I. 5. 5. Studies on both total porphyrins formed and their distribution were performed in hemolysates from cases of non-hereditary and hereditary PCT and AIP, before and after therapy. © 1980.Fil:Parera, V.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Fukuda, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.1980info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p947_PareraInt. J. Biochem. 1980;12(5-6):947-953reponame:Biblioteca Digital (UBA-FCEN)instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesinstacron:UBA-FCENenginfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/2.5/ar2025-09-29T13:42:51Zpaperaa:paper_0020711X_v12_n5-6_p947_PareraInstitucionalhttps://digital.bl.fcen.uba.ar/Universidad públicaNo correspondehttps://digital.bl.fcen.uba.ar/cgi-bin/oaiserver.cgiana@bl.fcen.uba.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:18962025-09-29 13:42:53.153Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturalesfalse
dc.title.none.fl_str_mv Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humans
title Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humans
spellingShingle Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humans
Parera, V.E.
ammonia lyase
Ammonia Lyases
porphobilinogen deaminase
porphobilinogen synthase
porphyrin
acute disease
article
biosynthesis
blood
enzymology
erythrocyte
human
newborn
porphyria
reference value
skin disease
Acute Disease
Ammonia-Lyases
Erythrocytes
Human
Hydroxymethylbilane Synthase
Infant, Newborn
Porphobilinogen Synthase
Porphyria
Porphyrins
Reference Values
Skin Diseases
Support, Non-U.S. Gov't
title_short Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humans
title_full Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humans
title_fullStr Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humans
title_full_unstemmed Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humans
title_sort Porphyrin biosynthesis and enzymic studies in erythrocytes from normals and porphyric humans
dc.creator.none.fl_str_mv Parera, V.E.
Stella, A.M.
De Xifra, E.A.W.
Fukuda, H.
Del C. Batlle, A.M.
author Parera, V.E.
author_facet Parera, V.E.
Stella, A.M.
De Xifra, E.A.W.
Fukuda, H.
Del C. Batlle, A.M.
author_role author
author2 Stella, A.M.
De Xifra, E.A.W.
Fukuda, H.
Del C. Batlle, A.M.
author2_role author
author
author
author
dc.subject.none.fl_str_mv ammonia lyase
Ammonia Lyases
porphobilinogen deaminase
porphobilinogen synthase
porphyrin
acute disease
article
biosynthesis
blood
enzymology
erythrocyte
human
newborn
porphyria
reference value
skin disease
Acute Disease
Ammonia-Lyases
Erythrocytes
Human
Hydroxymethylbilane Synthase
Infant, Newborn
Porphobilinogen Synthase
Porphyria
Porphyrins
Reference Values
Skin Diseases
Support, Non-U.S. Gov't
topic ammonia lyase
Ammonia Lyases
porphobilinogen deaminase
porphobilinogen synthase
porphyrin
acute disease
article
biosynthesis
blood
enzymology
erythrocyte
human
newborn
porphyria
reference value
skin disease
Acute Disease
Ammonia-Lyases
Erythrocytes
Human
Hydroxymethylbilane Synthase
Infant, Newborn
Porphobilinogen Synthase
Porphyria
Porphyrins
Reference Values
Skin Diseases
Support, Non-U.S. Gov't
dc.description.none.fl_txt_mv 1. 1. Studies on porphyrin biosynthesis from exogenus ALA, at various time intervals as well as direct enzyme measurements (aminolevulimc acid dehydratase (ALA-D); porphobilinogenase (PBG ase) and deaminase were carried out in hemolysates of human erythrocytes from healthy controls and patients with lead poisoning (Pb), acute intermittent porphyria (AIP), porphyria cutanea tarda (PCT), erythropoietic protoporphyria (EPP), variegate porphyria (VP) and congenital erythropoietic porphyria (CEP). 2. 2. Inhibited ALA-D in Pb, reduced PBGase and deaminase in AIP, lower uroporphyrinogen decarboxylase in PCT, and diminished isomerase in CEP, were confirmed. In addition, ALA-D was found, reduced in AIP, unchanged in PCT and increased in EPP, VP and CEP. PBGase and deaminase were, on the other hand, increased in Pb and PCT, unchanged in VP and diminished in EPP and CEP. 3. 3. Total porphyrin biosynthesis is a function of time; compared to normals, is lower in CEP and AIP, but higher in PCT. 4. 4. The porphyrin profile changes along the time; uroporphyrin increases at longer intervals while that of coproporphyrin concomitantly diminished. A significance enhancement of octacarboxylic porphyrins was observed during the entire duration of the incubation in PCT hemolysates. In CEP the main porphyrin was always uroporphyrin I. 5. 5. Studies on both total porphyrins formed and their distribution were performed in hemolysates from cases of non-hereditary and hereditary PCT and AIP, before and after therapy. © 1980.
Fil:Parera, V.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Stella, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Fukuda, H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
description 1. 1. Studies on porphyrin biosynthesis from exogenus ALA, at various time intervals as well as direct enzyme measurements (aminolevulimc acid dehydratase (ALA-D); porphobilinogenase (PBG ase) and deaminase were carried out in hemolysates of human erythrocytes from healthy controls and patients with lead poisoning (Pb), acute intermittent porphyria (AIP), porphyria cutanea tarda (PCT), erythropoietic protoporphyria (EPP), variegate porphyria (VP) and congenital erythropoietic porphyria (CEP). 2. 2. Inhibited ALA-D in Pb, reduced PBGase and deaminase in AIP, lower uroporphyrinogen decarboxylase in PCT, and diminished isomerase in CEP, were confirmed. In addition, ALA-D was found, reduced in AIP, unchanged in PCT and increased in EPP, VP and CEP. PBGase and deaminase were, on the other hand, increased in Pb and PCT, unchanged in VP and diminished in EPP and CEP. 3. 3. Total porphyrin biosynthesis is a function of time; compared to normals, is lower in CEP and AIP, but higher in PCT. 4. 4. The porphyrin profile changes along the time; uroporphyrin increases at longer intervals while that of coproporphyrin concomitantly diminished. A significance enhancement of octacarboxylic porphyrins was observed during the entire duration of the incubation in PCT hemolysates. In CEP the main porphyrin was always uroporphyrin I. 5. 5. Studies on both total porphyrins formed and their distribution were performed in hemolysates from cases of non-hereditary and hereditary PCT and AIP, before and after therapy. © 1980.
publishDate 1980
dc.date.none.fl_str_mv 1980
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p947_Parera
url http://hdl.handle.net/20.500.12110/paper_0020711X_v12_n5-6_p947_Parera
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/2.5/ar
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/2.5/ar
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv Int. J. Biochem. 1980;12(5-6):947-953
reponame:Biblioteca Digital (UBA-FCEN)
instname:Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
reponame_str Biblioteca Digital (UBA-FCEN)
collection Biblioteca Digital (UBA-FCEN)
instname_str Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron_str UBA-FCEN
institution UBA-FCEN
repository.name.fl_str_mv Biblioteca Digital (UBA-FCEN) - Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
repository.mail.fl_str_mv ana@bl.fcen.uba.ar
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