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Haemoprotein terminal oxidases in the nematodes Nippostrongylus brasiliensis and Ascaridia galli

Paget, T A, Fry, M and Lloyd, D ORCID: https://orcid.org/0000-0002-5656-0571 1988. Haemoprotein terminal oxidases in the nematodes Nippostrongylus brasiliensis and Ascaridia galli. Biochemical Journal 256 (1) , pp. 295-298. 10.1042/bj2560295

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Abstract

1. Mitochondria isolated from the gut-dwelling nematodes Nippostrongylus brasiliensis and Ascaridia galli (muscle and gut + reproductive tissue) were examined for cytochromes, and it was observed that N. brasiliensis and A. galli muscle tissue mitochondria contained a-, b- and c-type cytochromes, but their stoichiometries were quite different (1:2:1.9 and 1:11.4:13.6 respectively); A. galli gut + reproductive-tissue mitochondria, however, only contained b and c cytochromes, in a ratio of 1:0.8. 2. CO difference spectra showed the presence of CO-reacting b-type cytochrome(s) in all three types of mitochondria; the fast-reacting species comprised 30, 44 and 39% of the total in N. brasiliensis, A. galli muscle and A. galli gut + reproductive-tissue mitochondria respectively. 3. Cytochrome aa3 was observed in N. brasiliensis mitochondria and in those from A. galli muscle, but was below the level of detectability (less than 0.005 nmol/mg of protein) for A. galli gut + reproductive-tissue mitochondria. 4. Photochemical action spectra for the reversal of CO inhibition of the endogenous respiration of whole worms (at 24 microM- and 40 microM-O2 respectively for N. brasiliensis and A. galli) gave maxima at 598 and 542-543 nm, corresponding to the alpha- and beta-absorption maxima of cytochrome aa3, and at 567 nm (b-type cytochrome) for both worms. These results suggest that cytochrome aa3 is the major functional oxidase in N. brasiliensis, whereas the CO-reacting b-type cytochrome dominates in A. galli.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
Publisher: Portland Press
ISSN: 0264-6021
Last Modified: 26 Oct 2022 08:38
URI: https://orca.cardiff.ac.uk/id/eprint/127958

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