@article{6b126215d58d4a1cbef40ad3d160c2c1,
title = "Purification of human erythrocyte pyruvate kinase.",
author = "Chern, {C. J.} and Rittenberg, {M. B.} and Black, {J. A.}",
note = "Funding Information: The constants obtained in this laboratory are nearly identical with the values reported by McQUATE AND UTTER 7 for rabbit muscle enzyme: Km for ADP, 3{"} lO-4 M; Km for PEP, 7' lO-5 M (pH 7.5, 300) • Although the Km for ADP is essentially the same for the two enzymes, Km for PEP is almost an order of magnitude larger for red cell pyruvate kinase than it is for rabbit muscle enzyme. This research was supported by Grant AM 02612 from the National Institutes of Health. Funding Information: This investigation was supported by United States Public Health Service Grant AM 00567, by Research Career Award AM-K6-2oI8 from the National Institute of Arthritis and Metabolic Diseases of the National Institutes of Health, United States Public Health Service, by United States Atomic Energy Commission Contract AT(3o-1)-9Ol with the New England Deaconess Hospital (NY0-9oi-57), and by Public Health Service International Postdoctoral Research Fellowship I FO5-TW-74I.",
year = "1972",
month = nov,
day = "25",
language = "English (US)",
volume = "247",
pages = "7173--7180",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "22",
}