Abstract
Human α-lactalbumin has not been described as a glycoprotein, despite the fact that several α-lactalbumins of both ruminant and nonruminant species are known to be glycosylated. In all these species the glycosylation site is the 45Asn in the usual triplet 45Asn–Gly/Gln–47Ser. We have found that human α-lactalbumin is glycosylated and the glycosylation site has been determined by protein sequencing and mass spectrometry. We report an unusual glycosylation site at 71Asn in the triplet 71Asn–Ile–73Cys, which is conserved in all known α-lactalbumins except red-necked wallaby. That a relatively small proportion of the protien is glycosylated (about 1%) may reflect the importance of this region of the protein sequence to the molten globule state of α-lactalbumin.
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Giuffrida, M.G., Cavaletto, M., Giunta, C. et al. The Unusual Amino Acid Triplet Asn–Ile–Cys Is a Glycosylation Consensus Site in Human α-Lactalbumin. J Protein Chem 16, 747–753 (1997). https://doi.org/10.1023/A:1026359715821
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DOI: https://doi.org/10.1023/A:1026359715821