Abstract
KARL ZEILE1 in 1930 was the first to provide evidence that the catalytic activity towards hydrogen peroxide of purified preparations obtained from liver and from marrow seedlings is intimately connected with a pigment exhibiting the spectral behaviour of a complex consisting of a hæmatin group—the iron being stabilised in the trivalent state—and of a colloidal component. The position of the absorption bands of the pyridine hæmochromogen and of the porphyrin, obtained in solution by treatment with hydrazine and acetic acid, led him to conclude that the hænatin contained in the enzyme complex was cither identical with, or was an isomer of, the prosthetic group of natural hæmoglobin.
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References
K. Zeile and H. Hellström, Z. physiol. Chem., 192, 171; 1930. 195, 39; 1931.
R. Hill and D. Keilin, Proc. Roy. Soc., B, 107, 286; 1930.
K. Zeile and F. Reuter, Z. physiol. Chem., 221, 101; 1933.
K. G. Stern, ibid., 208, 86, 212, 207; 1932. 215, 35, 217, 237 219, 105; 1933.
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STERN, K. Constitution of the Prosthetic Group of Catalase. Nature 136, 302 (1935). https://doi.org/10.1038/136302a0
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DOI: https://doi.org/10.1038/136302a0
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