Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1924 Apr 30;39(5):757-75.
doi: 10.1084/jem.39.5.757.

STUDIES ON OXIDATION AND REDUCTION BY PNEUMOCOCCUS : V. THE DESTRUCTION OF OXYHEMOGLOBIN BY STERILE EXTRACTS OF PNEUMOCOCCUS

J M Neill  1 , O T Avery
Affiliations

STUDIES ON OXIDATION AND REDUCTION BY PNEUMOCOCCUS : V. THE DESTRUCTION OF OXYHEMOGLOBIN BY STERILE EXTRACTS OF PNEUMOCOCCUS

J M Neill et al. J Exp Med. .

Abstract

1. Sterile broth extracts of unwashed pneumococci actively destroy hemoglobin to methemoglobin and lower degradation products. 2. Sterile saline extracts of washed pneumococci do not by themselves form methemoglobin; extracts of this type may be completed or activated by the addition of certain complementary substances such as meat infusion and yeast extract. 3. The hemoglobin-destroying activity of pneumococcus extract is lost by exposure to 65 degrees C. for 10 minutes. 4. The properties of an extract upon which these blood changes depend are related to other known oxidation-reduction functions of the same extract. 5. Oxyhemoglobin is converted to methemoglobin only by cell extracts in the reduced form; completely oxidized extracts are inactive in the presence of blood. The action of hydrogen peroxide and the influence of blood catalase on these reactions are discussed. 6. During the reaction between oxyhemoglobin and pneumococcus extract oxygen is consumed. 7. The mechanism of methemoglobin formation by pneumococcus is interpreted as an oxidation process in which deoxygenation of oxyhemoglobin and peroxide formation occur as intermediary reactions. The active agent of the oxidation of hemoglobin is considered to be a peroxide of bacterial origin.

PubMed Disclaimer

References

    1. J Exp Med. 1924 Mar 31;39(4):543-52 - PubMed
    1. J Exp Med. 1924 Feb 29;39(3):347-55 - PubMed
    1. J Exp Med. 1921 Apr 30;33(5):627-40 - PubMed
    1. J Exp Med. 1924 Apr 30;39(5):745-55 - PubMed
    1. J Exp Med. 1913 May 1;17(5):587-92 - PubMed