|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
Journal of Cell Science, Vol 16, 623-637, Copyright © 1974 by Company of Biologists
Submitted on May 7, 1974
1 Department of Biological Sciences, The University, Dundee DD1 4HN, Scotland; The Institute of Biology, Hacettepe University, Ankara, Turkey
2 Department of Biological Sciences, The University, Dundee DD1 4HN, Scotland
Attempts were made to localize the following enzymes within bacteroids and host tissue: reduced-NAD oxidoreductase, succinate oxidoreductase, adenosinetriphosphate phosphorylase, diaminobenzidine oxidase, and xylylene diamine oxidase. Diaminobenzidine (DAB) staining was localized within the mitochondrial membranes and within the bacteroid cytomembrane and associated vesicles, whereas dehydrogenase enzymes within the bacteroids were for the greater part mesosomal. Peroxidative reduction of DAB and xylylene diamine within the bacteroid nuclear regions occurred in the presence of catalase, to which the cytomembrane appeared to be impermeable. A cyanide-insensitive oxidase localized within the bacteroid mesosomes and nuclear regions was not affected by the addition of catalase, aminotriazole or pyruvate. Ca2+-stimulated ATP-phosphorylase was localized within the bacteroid cytomembrane, whereas a Mg2+-stimulated ATP-phosphorylase was localized within the host cell plasma membrane.
Submitted on May 7, 1974