Purification and Characterization of an Intracellular Dipeptidase from Mycobacterium phlei
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چکیده
منابع مشابه
Purification and characterization of dihydrofolate reductase from Mycobacterium phlei.
The dihydrofolate reductase from Mycobacterium phlei was purified and characterized; it has an Mr of 15 000 and a pI of 4.8. It is competitively inhibited by both methotrexate and trimethoprim, although the affinity is less than for other bacterial dihydrofolate reductases.
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Aim: DNA topoisomerases control several cellular activities by catalyzing the relaxation of superhelices, which are produced during the replication of DNA. Investigation of the inhibitory action of the candidate substances on topoisomerase activity is widely used in drug development. The purpose of this study was to purify topoisomerase I from Mycobacterium phlei, which is closely related to My...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1972
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1972.tb01917.x