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
- Institución
- Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
- OAI Identificador
- paperaa:paper_0020711X_v12_n5-6_p947_Parera
Ver los metadatos del registro completo
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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 http://purl.org/coar/resource_type/c_6501 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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1844618733693173760 |
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13.070432 |