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Heat‐labile uracil‐DNA glycosylase: purification and characterization
Author(s) -
Sobek H.,
Schmidt M.,
Frey B.,
Kaluza K.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00444-9
Subject(s) - uracil dna glycosylase , uracil , dna glycosylase , chemistry , glycerol , dna , biochemistry , escherichia coli , enzyme , dna repair , gene
A uracil‐DNA glycosylase (UNG) from a psychrophilic marine bacterium (BMTU 3346) has been purified to apparent homogeneity. The enzyme has a molecular weight of 23 400 Da. It is stable in complex buffers (containing glycerol/BSA), whereas it is heat‐labile in dilute buffers (free of stabilizers) with a half‐life of 2 min at 40°C. Due to the thermolability, uracil‐DNA glycosylase is suitable for application in the carryover prevention technique showing less residual activity and/or a slower reactivation rate than the usually applied UNG from Escherichia coli .