Difference spectroscopic characterisation of the cytochrome complement in Acanthocheilonema viteae
Mendis, A.H.W., Armson, A. and Grubb, W.B. (1992) Difference spectroscopic characterisation of the cytochrome complement in Acanthocheilonema viteae. Molecular and Biochemical Parasitology, 52 (2). pp. 159-166.
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(Dithionite-reduced) minus (ferricyanide-oxidised) difference spectra of 600 × g and 12 000 × g subcellular pellet fractions of adult male Acanthocheilonema viteae exhibited α-absorption maxima (296 K) attributable to Cyt c555, Cyt b562 and aa3 (600–605 nm). The γ(Soret) maximum of both fractions was evident at 427 nm, with a shoulder at 432–434 nm. 600 × g and 12 000 × g pellet fractions of adult female and mixed-sex adult A. viteae exhibited similar absorption maxima. (Succinate-reduced) — (ferricyanide-oxidised) difference spectra of the 12 000 × g pellet fraction of mixed-sex adult A. viteae showed absorption maxima at 555 and 562 nm, 600 and 630 nm, suggesting the reduction of Cyt c555, Cyt b562, Cyt aa3 (600 nm) and an unidentified species (630 nm peak) Antimycin A (10′-6 M) induced the disappearance of the maxima at the maxima at 555, 600 and 630 nm corresponding to Cyt c555, Cyt aa3 and the unidentified species; the maximum at 562 nm prevailed in the presence of antimycin A. These antimycin A induced changes can be cited as classical evidence for the functional involvement of these a, b and c type cytochromes in respiratory electron transport. (Dithionite reduced + CO) — (dithionite reduced) difference spectra suggest that adult A. viteae may have one or more CO-binding-species, one of which appears to be a low-spin-haemoprotein with a b-type or c-type haem, which has essentially an electron carrier function rather than a ligand binding function.
|Publication Type:||Journal Article|
|Copyright:||1992 Elsevier Science Publishers B.V.|
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