A GENERAL METHOD OF PURIFICATION OF ADENOSINE DEAMINASE BY AFFINITY CHROMATOGRAPHY
| Autor: | Umberto Montali, Carlo Rossi, Antonio Lucacchini, Giovanni Ronca |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Electrophoresis
Adenosine Erythrocytes Duodenum Biochemistry Chromatography Affinity chemistry.chemical_compound Adenosine deaminase Intestinal mucosa Affinity chromatography Aminohydrolases medicine Animals Humans Intestinal Mucosa Cellulose chemistry.chemical_classification Chromatography biology Chemistry Elution Adenine Enzyme biology.protein Agarose Cattle Chickens Spleen medicine.drug |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1975.tb02416.x |
| Popis: | Affinity chromatography has been used to purify adenosine deaminase from various sources: calf spleen, calf intestinal mucosa, chicken duodena and human erythrocytes. For this purpose a specific inhibitor, 9-(p-aminobenzyl) adenine, was synthesized and covalently joined to agarose. Adenosine deaminase is selectively retained by such an inhibitor-resin when highly impure solutions are chromatographed through it. After elution from the resin with guanylurea, a competitive inhibitor, the enzyme is homogeneous and can be recovered in yields of 80 percent or more and the same number of multiple forms of the enzyme is present in the purified preparation and in the crude extract. |
| Databáze: | OpenAIRE |
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