Multiple conformations of deoxyribonuclease A. Their separation at alkaline pH and low ionic strength in the presence of Ca2+.
Biochim Biophys Acta
; 579(2): 298-302, 1979 Aug 28.
Article
in En
| MEDLINE
| ID: mdl-43741
ABSTRACT
Gel filtration on Sephadex G-100 at pH 9.0 in 1 mM Tris buffer produces denaturation and inactivation of pancreatic DNAase A. Limiting concentrations of Ca2+ in the suspension and elution buffer, reactivates some of the enzyme molecules in an amount proportional to the calcium added. Stable active and inactive forms were separated on Sephadex columns. A model for the conformational role of Ca2+ on DNAase A demonstrates that at least one Ca2+ is involved (Kapp = 8.3 . 10(-5) M) in the correct folding of the polypeptide chain. Na+ was unable to reactivate the enzyme.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Calcium
/
Deoxyribonucleases
Type of study:
Prognostic_studies
Language:
En
Journal:
Biochim Biophys Acta
Year:
1979
Document type:
Article