Cary P D
Biochem J. 1982 Dec 1;207(3):519-27. doi: 10.1042/bj2070519.
Two new, closely similar, acidic proteins were extracted and purified from calf thymus and designated AP-X and AP-Y (acidic proteins X and Y). They contain about 33% acidic residues, mostly non-amidated, and 20% lysine, but no arginine, tyrosine, histidine or tryptophan. There is a single phenylalanine residue in a molecular weight of approx. 5000. Circular dichroism and proton nuclear magnetic resonance show that they do not take up secondary or tertiary structure in free solution, as expected from the low content of hydrophobic amino acids. They appear structurally related to the high-mobility-group proteins HMG 14 and 17. Controlled extraction experiments indicate that proteins AP-X and AP-Y are at least partially located in the calf thymus nucleus.
从犊牛胸腺中提取并纯化出两种新的、极为相似的酸性蛋白质，分别命名为AP-X和AP-Y（酸性蛋白质X和Y）。它们含有约33%的酸性残基，大部分未酰胺化，还有20%的赖氨酸，但不含精氨酸、酪氨酸、组氨酸或色氨酸。在分子量约为5000的分子中存在一个苯丙氨酸残基。圆二色性和质子核磁共振表明，正如疏水性氨基酸含量低所预期的那样，它们在游离溶液中不具有二级或三级结构。它们在结构上似乎与高迁移率族蛋白HMG 14和17相关。控制提取实验表明，蛋白质AP-X和AP-Y至少部分位于犊牛胸腺细胞核中。
