Myoglobin Species with Enhanced Prooxidative Activity Is Formed during Mild Proteolysis by Pepsin-Reference-Cited by-同舟云学术

Myoglobin Species with Enhanced Prooxidative Activity Is Formed during Mild Proteolysis by Pepsin

Published:2004-02-21 Issue:6 Volume:52 Page:1675-1681
ISSN:0021-8561
Container-title:Journal of Agricultural and Food Chemistry
language:en
Short-container-title:J. Agric. Food Chem.

Author:

Carlsen Charlotte U.¹,Skibsted Leif H.¹

Affiliation:

1. Department of Dairy and Food Science, Food Chemistry, Royal Veterinary and Agricultural University, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark

Publisher

American Chemical Society (ACS)

Subject

General Agricultural and Biological Sciences,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jf030494u

Reference28 articles.

1. Redox Reactions of Hemoglobin and Myoglobin: Biological and Toxicological Implications

2. Effect of pH on Lipid Oxidation Using Trout Hemolysate as a Catalyst: A Possible Role for Deoxyhemoglobin

3. The effects of pH on the mechanism of hydrogen peroxide and lipid hydroperoxide consumption by myoglobin: a role for the protonated ferryl species

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