Dye-induced fluorescence of tumour cells: photochemical action spectra

1974 ◽  
Vol 6 (3) ◽  
pp. 237-243 ◽  
Author(s):  
A. L. Bastos ◽  
D. Marques ◽  
M. A. Affra
1983 ◽  
Vol 210 (3) ◽  
pp. 721-725 ◽  
Author(s):  
R I Scott ◽  
D Lloyd

1. Room-temperature CO-reduced minus reduced difference spectra of intact cells of Acanthamoeba castellanii show the presence of CO-reacting haemoproteins in cells from the early-exponential, late-exponential and stationary phases of growth. 2. The relative rates of reaction with CO of the two haemoproteins differ; that of cytochrome a/a3 with CO is complete within 1 min of bubbling with CO, whereas that of cytochrome b takes longer than 90 min. 3. Photochemical action spectra reveal cytochrome a/a3 as the predominant haemoprotein oxidase at all stages of growth. 4. It is concluded that the alternative oxidases known to be present in these organisms are not cytochromes.


1988 ◽  
Vol 256 (1) ◽  
pp. 295-298 ◽  
Author(s):  
T A Paget ◽  
M Fry ◽  
D Lloyd

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.


1980 ◽  
Vol 105 (1) ◽  
pp. 177-185 ◽  
Author(s):  
Paul S. HOFFMAN ◽  
Richard M. IRWIN ◽  
L. A. CARREIRA ◽  
T. Vance MORGAN ◽  
Burt D. ENSLEY ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document