Manson W, Carolan T, Annan W D
Eur J Biochem. 1977 Sep;78(2):411-7. doi: 10.1111/j.1432-1033.1977.tb11753.x.
After consideration of its electrophoretic behaviour, amino acid composition and phosphate content, bovine alpha s0 casein has been shown to differ from alpha s1 casein only in respect of its phosphate content. The presence in alpha s0 casein of one phosphate residue more than occurs in alpha s1 casein was confirmed by comparative degradative studies performed on both proteins. From these it was concluded that alpha s0 casein may be considered as being alpha s1 casein which has been modified by phosphorylation of the seryl residue located at position 41.
在对其电泳行为、氨基酸组成和磷酸盐含量进行研究后发现,牛αs0酪蛋白与αs1酪蛋白的差异仅在于其磷酸盐含量。通过对这两种蛋白质进行的比较降解研究,证实了αs0酪蛋白中磷酸盐残基比αs1酪蛋白多一个。由此得出结论,αs0酪蛋白可被视为αs1酪蛋白在位于第41位的丝氨酰残基发生磷酸化修饰后的产物。