Access the full text.
Sign up today, get DeepDyve free for 14 days.
(1937)
Studies on biological oxidation
(1938)
Biochem. Z. V. R. Cancer Research
(1937)
Anat. Rec
J. Biol. Chem
(1940)
Science
(1942)
Gen. Pt~ysiol
J. Clarke (1907)
MedicineBristol Medico-Chirurgical Journal (1883), 25
(1940)
Biol. Chem. Potter, V. R., ]. Biol. Chem
(1939)
Biochem. J
1. The effect of ribonuclease on various enzyme systems was studied as one approach to the problem of whether or not these enzymes are contained in macromolecules of ribonucleoprotein nature in protoplasm. 2. Ribonuclease inhibited CoI-cytochrome c reductase, succinic dehydrogenase, and cytochrome oxidase, all of which require cytochrome c in order to function. Ribonuclease did not act on cytochrome c . 3. Ribonuclease did not inhibit urease, xanthine oxidase, catalase, alkaline phosphatase, or adenosine triphosphatase under the conditions employed. 4. It was suggested that ribonuclease acted sterically by preventing contact between cytochrome c and its activating centers. 5. It was suggested that the enzymes inhibited may be contained in a ribonucleoprotein of macromolecular dimensions but that the enzymes not inhibited are not necessarily excluded from such a complex by the data presented. 6. Further evidence against the Szent-Györgyi theory of hydrogen transport was presented and discussed. Footnotes Submitted: 25 January 1943
The Journal of General Physiology – Rockefeller University Press
Published: May 20, 1943
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.