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Biomedical subjects

M Ishaque

Publications and source records attributed to M Ishaque.

At least 55 records · Page 3Linked to original sources
PubMed1975

Cytochrome pigments in Mycobacterium leprae isolated from armadillos (Dasypus novemcinctus L.).

The bacilli were isolated from granulomata harvested from armadillos. Cytochrome systems in whole cell suspensions as well as in cell-free extracts were examined spectrophotometrically. The intact cells contained cytochromes of the a+b3, b and c type which were found to be present mainly in the reduced form. The cytochrome systems in cell-free extracts of M. leprae were in the oxidized form but contained the same type of cytochromes as the intact bacteria. The presence of cytochromes was easily detectable in the anaerobically-reduced (no substrate added) as well as in the dithionite- or succinate-reduced minus O2-oxidized difference spectra. The dithionite-reduced plus CO minus reduced difference spectra exhibited cytochromes a3 and o monoxide binding pigments.

Animals↗
PubMed1975

Oxidation of reduced nicotinamide adenine dinucleotide by particles from Mycobacterium lepraemurium.

Particles from Mycobacterium lepraemurium catalysed the oxidation of NADH with oxygen as the terminal electron acceptor. The preparations contained cytochromes of the a + a3'b and c types, as well as CO-binding pigments. The NADH oxidase activity was sensitive to inhibitors of the flavoprotein system as well as to HQNO and antimycin A. In addition, a cytochrome oxidase sensitive to cyanide was also present. The system was inhibited by the thiol-binding agent, PCMB, and thus indicated the involvement of sulphydryl group in the enzymatic oxidation of NADH. The sensitivity of the NADH oxidase system to all the inhibitors of the respiratory chain and the effect of these inhibitors on the absorption spectra suggested that cytochromes of the b, c, a + a3 types are involved in the transfer of electrons in NADH oxidation.

Amobarbital↗