异常氨基酸三联体天冬酰胺-异亮氨酸-半胱氨酸是人类α-乳白蛋白中的一个糖基化共有序列位点。
The unusual amino acid triplet Asn-Ile-Cys is a glycosylation consensus site in human alpha-lactalbumin.
作者信息
Giuffrida M G, Cavaletto M, Giunta C, Neuteboom B, Cantisani A, Napolitano L, Calderone V, Godovac-Zimmermann J, Conti A
机构信息
Centro Studio Alimentazione Animali, CNR, Torino, Italy.
出版信息
J Protein Chem. 1997 Nov;16(8):747-53. doi: 10.1023/a:1026359715821.
Human alpha-lactalbumin has not been described as a glycoprotein, despite the fact that several alpha-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 alpha-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 alpha-lactalbumins except red-necked wallaby. That a relatively small proportion of the protein is glycosylated (about 1%) may reflect the importance of this region of the protein sequence to the molten globule state of alpha-lactalbumin.
尽管已知反刍动物和非反刍动物的几种α-乳白蛋白是糖基化的，但人α-乳白蛋白尚未被描述为糖蛋白。在所有这些物种中，糖基化位点是通常三联体45Asn-Gly/Gln-47Ser中的45Asn。我们发现人α-乳白蛋白是糖基化的，并且糖基化位点已通过蛋白质测序和质谱法确定。我们报告了三联体71Asn-Ile-73Cys中71Asn处一个不寻常的糖基化位点，除红颈小袋鼠外，该位点在所有已知的α-乳白蛋白中都是保守的。蛋白质中相对较小比例（约1%）被糖基化，这可能反映了该蛋白质序列区域对α-乳白蛋白熔球状态的重要性。
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