Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography
1. 1. Fully reversible and highly stable biospecific adsorbents have been prepared by attaching delta aminolaevulinate to cyanogen bromide activated-Sepharose 4B, either directly or through extension arms. 2. 2. Purification of bovine liver delta aminolaevulinate dehydratase by means of these select...
Guardado en:
| Publicado: |
1977
|
|---|---|
| Materias: | |
| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v8_n5_p353_Stella http://hdl.handle.net/20.500.12110/paper_0020711X_v8_n5_p353_Stella |
| Aporte de: |
| id |
paper:paper_0020711X_v8_n5_p353_Stella |
|---|---|
| record_format |
dspace |
| spelling |
paper:paper_0020711X_v8_n5_p353_Stella2023-06-08T14:41:16Z Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography liver enzyme porphobilinogen synthase porphyrin cattle in vitro study methodology theoretical study 1. 1. Fully reversible and highly stable biospecific adsorbents have been prepared by attaching delta aminolaevulinate to cyanogen bromide activated-Sepharose 4B, either directly or through extension arms. 2. 2. Purification of bovine liver delta aminolaevulinate dehydratase by means of these selective adsorbents is reported. These materials adsorb the enzyme quantitatively from partially purified preparations, and elution of delta aminolaevulinate dehydratase is achieved by modifying the ionic strength of the buffer. © 1977. 1977 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v8_n5_p353_Stella http://hdl.handle.net/20.500.12110/paper_0020711X_v8_n5_p353_Stella |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
liver enzyme porphobilinogen synthase porphyrin cattle in vitro study methodology theoretical study |
| spellingShingle |
liver enzyme porphobilinogen synthase porphyrin cattle in vitro study methodology theoretical study Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography |
| topic_facet |
liver enzyme porphobilinogen synthase porphyrin cattle in vitro study methodology theoretical study |
| description |
1. 1. Fully reversible and highly stable biospecific adsorbents have been prepared by attaching delta aminolaevulinate to cyanogen bromide activated-Sepharose 4B, either directly or through extension arms. 2. 2. Purification of bovine liver delta aminolaevulinate dehydratase by means of these selective adsorbents is reported. These materials adsorb the enzyme quantitatively from partially purified preparations, and elution of delta aminolaevulinate dehydratase is achieved by modifying the ionic strength of the buffer. © 1977. |
| title |
Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography |
| title_short |
Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography |
| title_full |
Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography |
| title_fullStr |
Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography |
| title_full_unstemmed |
Porphyrin biosynthesis-Immobilized enzymes and ligands-V. Purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography |
| title_sort |
porphyrin biosynthesis-immobilized enzymes and ligands-v. purification of aminolaevulinate dehydratase from bovine liver by affinity chromatography |
| publishDate |
1977 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v8_n5_p353_Stella http://hdl.handle.net/20.500.12110/paper_0020711X_v8_n5_p353_Stella |
| _version_ |
1768543069291937792 |