Lozier J, Takahashi N, Putnam F W
Proc Natl Acad Sci U S A. 1984 Jun;81(12):3640-4. doi: 10.1073/pnas.81.12.3640.
We have determined the complete amino acid sequence of beta 2-glycoprotein I (Mr, congruent to 50,000), a human plasma protein that is associated with lipids and binds to platelets but whose function is not yet known. The protein consists of 326 amino acids and has five attached glucosamine-containing oligosaccharides. The protein is rich in cysteine and proline, and the sequence is notable for the frequent occurrence of Cys-Pro linkages at regular intervals. Computerized analysis of the sequence reveals five consecutive homologous segments in which cysteine, proline, and tryptophan appear to be highly conserved. This suggests that beta 2-glycoprotein I may have evolved by repeated duplications of a gene coding for a 60-amino acid segment of protein.
我们已经确定了β2-糖蛋白I(分子量约为50,000)的完整氨基酸序列,它是一种与脂质相关且能与血小板结合的人血浆蛋白,但其功能尚不清楚。该蛋白质由326个氨基酸组成,并含有5个连接的含葡萄糖胺的寡糖。该蛋白质富含半胱氨酸和脯氨酸,其序列以规则间隔频繁出现的半胱氨酸-脯氨酸连接为显著特征。对该序列的计算机分析揭示了五个连续的同源片段,其中半胱氨酸、脯氨酸和色氨酸似乎高度保守。这表明β2-糖蛋白I可能是通过编码60个氨基酸蛋白质片段的基因的重复复制而进化而来的。