Immobilized pronase
Pronase was successfully coupled to an arylamino derivative of porous glass. The immobilized enzyme retains considerable activity against large and small substrates: bovine serum albumin, 57%; benzoyl-L-arginine ethylester, 27%; L-leucine-p-nitroanilide, 67%. Studies of enzyme stability, pH behavior...
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Veröffentlicht in: | Biochemical and biophysical research communications 1971-07, Vol.44 (2), p.426-432 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | Pronase was successfully coupled to an arylamino derivative of porous glass. The immobilized enzyme retains considerable activity against large and small substrates: bovine serum albumin, 57%; benzoyl-L-arginine ethylester, 27%; L-leucine-p-nitroanilide, 67%. Studies of enzyme stability, pH behavior and temperature dependence are presented. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/0006-291X(71)90618-8 |