FREDERICK L. BENOIT; GEORGE B. THEIL, M.D.; RAYMOND H. WATTEN
The presence of a muscle heme protein distinct from adult myoglobin was first shown in fetal calves' hearts by Jonxis and Wadman (1) in 1952. Subsequently, "fetal" myoglobin was identified in human newborn muscle, and its replacement by adult myoglobin in the first 6 months of life was shown (2). These proteins differ in their electrophoretic mobilities and solubility in ammonium sulfate; fetal myoglobin is less soluble in ammonium sulfate and has a faster rate of migration when subjected to electrophoresis than the adult protein. In addition, dissimilar absorption spectra have been noted between the two proteins (2, 3).
FREDERICK L. BENOIT, GEORGE B. THEIL, RAYMOND H. WATTEN. Myoglobinuria and Persistence of Fetal Myoglobin. Ann Intern Med. 1964;61:1133–1139. doi: 10.7326/0003-4819-61-6-1133
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Published: Ann Intern Med. 1964;61(6):1133-1139.
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