Abstract
IN 1961 Gregolin and Singer1 reported that yeast respiratory particles, prepared by mechanical disruption of cells in 1 per cent NaCl, do not oxidize D( — ) laetate with oxygen as the terminal electron acceptor. However, the particles exhibit strong D( — ) lactic dehydrogenase activity, and oxidize D( — ) laetate with oxygen uptake on addition of external cytochrome c. More recently, Gregolin and D'Alberton observed2 that D( — ) laetate is oxidized at high rate by oxygen when respiratory particles are prepared by disintegration of the cells in sucrose solution. When tested in a medium known to give maximal oxidase activity, the oxidation is not stimulated by addition of cytochrome c. In the presence of the same mixture (plus NaN3), D( — ) lactate is not oxidized by this preparation with cytochrome c as artificial electron acceptor.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Gregolin, C., and Singer, T. P., Biochem. and Biophys. Res. Comm., 4, 189 (1961).
Gregolin, C., and D'Alberton, A., Biochem. and Biophys. Res. Comm., 14, 103 (1964).
Roy, B. R., Nature, 201, 80 (1964).
Gregolin, C., and Singer, T. P., Biochim. Biophys. Acta, 67, 410 (1963).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
GREGOLIN, C., SCALELLA, P. & D'ALBERTON, A. Interaction of Cytochrome c with Yeast D(—) Lactic Oxidase. Nature 204, 1302–1303 (1964). https://doi.org/10.1038/2041302b0
Issue Date:
DOI: https://doi.org/10.1038/2041302b0
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.