Shomers J P, Tabak L A, Levine M J, Mandel I D, Ellison S A
J Dent Res. 1982 Jun;61(6):764-7. doi: 10.1177/00220345820610062201.
Members of a family of acidic proteins taken from human submandibular-sublingual saliva were designated cysteine-containing phosphoproteins, since they could be distinguished from other salivary phosphoproteins by the presence of half-cystine. These molecules consisted of a single peptide chain of approximately 14,000 daltons. Their isoelectric points ranged from 4.3 to 5.9. Two groups (C2 and C3) were O-phosphorylated. Their charge heterogeneity was apparently due to variations in content of phosphate and acidic and basic amino acids.
从人下颌下腺-舌下腺唾液中提取的一类酸性蛋白质成员被命名为含半胱氨酸磷蛋白,因为它们可通过半胱氨酸的存在与其他唾液磷蛋白区分开来。这些分子由一条约14,000道尔顿的单肽链组成。它们的等电点范围为4.3至5.9。两组(C2和C3)被O-磷酸化。它们的电荷异质性显然是由于磷酸盐以及酸性和碱性氨基酸含量的变化所致。