Formiminotransferase-cyclodeaminase from porcine liver: Purification and physical properties of the enzyme complex
A simple procedure for the purification of the formiminotransferase-cyclodeaminase enzyme complex is described. The crystalline preparation is homogeneous by ultracentrifugation and electrophoresis and appears to be composed of eight apparently identical subunits of about 6.4 × 10 4 daltons. Both en...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1975, Vol.169 (2), p.662-668 |
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| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
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| Online-Zugang: | Volltext |
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| Zusammenfassung: | A simple procedure for the purification of the formiminotransferase-cyclodeaminase enzyme complex is described. The crystalline preparation is homogeneous by ultracentrifugation and electrophoresis and appears to be composed of eight apparently identical subunits of about 6.4 × 10
4 daltons. Both enzyme activities migrate with the single protein band on electrophoresis and it is proposed that the activities are probably associated with different sites on one type of polypeptide chain. |
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| ISSN: | 0003-9861 1096-0384 |
| DOI: | 10.1016/0003-9861(75)90210-6 |