Abstract
Extract: Differences in sialic acid content and not genetic polymorphism determine the observed electrophoretic heterogeneity of human lactoferrin, the iron-binding protein of external secretions. Lactoferrin molecules have at least one to four sialic acid residues. The asialo derivative is electrophoretically homogeneous.
Speculation: As with other nonhuman iron-binding proteins from various species, human lactoferrin from several secretions was shown to have varying sialic acid content. A regulatory role of sialic acid in the regulation of secretion and function of lactoferrin is postulated.
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Wolfson, D., Robbins, J. Heterogeneity of Human Lactoferrin Due to Differences in Sialic Acid Content. Pediatr Res 5, 514–517 (1971). https://doi.org/10.1203/00006450-197110000-00003
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DOI: https://doi.org/10.1203/00006450-197110000-00003