Characterization Studies of Three Myoglobin Fractions from Bovine Musclea
- 1 July 1964
- journal article
- research article
- Published by Wiley in Journal of Food Science
- Vol. 29 (4) , 429-434
- https://doi.org/10.1111/j.1365-2621.1964.tb01756.x
Abstract
SUMMARY: Three electrophoretically and chromatographically distinct myoglobin fractions from beef muscle were compared as to absorption spectra, relative heme contents, susceptibility to acid cleavage of heme groups, and autoxidation rates. All 3 myoglobin fractions were found to have identical wavelength positions for minimum and maximum light absorption and to exhibit the same autoxidation rates. Different light absorptivity values and susceptibilities to acid cleavage for the 3 different myoglobins led to the tentative conclusion that structural variations existed at the porphyrin‐globin linkages.This publication has 17 references indexed in Scilit:
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