Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol.
FEBS Lett
; 303(1): 11-4, 1992 May 25.
Article
en En
| MEDLINE
| ID: mdl-1592107
ABSTRACT
Four derivatives of hen lysozyme, each lacking one native disulfide bond of the four in authentic lysozyme, were produced in Escherichia coli by expressing synthetic mutant genes. In the reoxidation reaction of the reduced derivatives purified from inclusion bodies, the addition of glycerol significantly enhanced the efficiency of folding and 'correct' disulfide bond formation. This enabled simple chromatographical purification of refolded materials. Purified 3SS-derivatives all showed lytic activities and secondary structures comparable to authentic lysozyme, which directly showed that none of the four native disulfide bonds is a prerequisite for 'correct' in vitro folding.
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Banco de datos:
MEDLINE
Asunto principal:
Muramidasa
/
Disulfuros
/
Glicerol
Límite:
Animals
Idioma:
En
Año:
1992
Tipo del documento:
Article