Isolation, purification and characterization of Cardiolipin synthase from Mycobacterium phlei {PRIVATE}.

ABSTRACT: It has been observed that mycobacterial species has high content of cardiolipin (CL) in their cell membranes more so pathogenic mycobacteria and in bacteria CL activates polymerases, gyrases by removing the bound ADP. Therefore, in the present study cardiolipin synthase (cls) which catalyses the formation of CL was isolated purified and characterized from the cell membrane of Mycobacterium phlei. The purified cls obtained from C-18 RP-HPLC column had a molecular weight of 58 kDa with an isoelectric point of 4.5. The enzyme activity (11.5+0.15 µM of CL phosphorous. ml-1 minute-1 for PG as substrate and 14+0.35µM of CL phosphorous. ml-1 minute-1 for CDP-DG as substrate) was optimal at pH 4.8 and showed KM values of 55+0.05µM and 2.56+0.04µM for phosphatidyl glycerol and CDP-diacylglycerol, r

SUBMITTER: Sarma PV 

PROVIDER: S-EPMC3732442 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature