Abstract
Homozygous cattle transferrin has been fractionated into six main peaks by DEAE-Sephadex chromatography. These correspond to the six transferrin components seen in starch gel electrophoresis of normal serum. In addition, six more minor components were isolated from DEAE-Sephadex, making 12 in all, and these could be divided into six pairs. Treatment of whole transferrin with neuraminidase yielded only two bands. Treatment of the individual fractionated bands showed that the slower band of each pair had the same mobility as the slow band from treated whole transferrin, while the faster band from each pair corresponded with the fast band of treated whole transferrin. These observations, and the results of sialic acid assays, showed that the difference between the pairs of bands was caused by differing numbers of sialic acid residues (0–5) per molecule of protein, but that sialic acid was not responsible for the difference between the bands within a pair. The mode of genetic control is discussed and probably involves three loci. Other physicochemical properties of cattle transferrins, namely, molecular weight, effect of iron addition, and behavior in isoelectric focusing, were also studied.
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