Scanu A M, Edelstein C
University of Chicago, South Maryland, IL 60637.
Clin Genet. 1994 Jul;46(1 Spec No):42-5. doi: 10.1111/j.1399-0004.1994.tb04200.x.
The size polymorphism of Lp(a) is well recognized. It is now apparent that there is an additional polymorphism resulting from mutations occurring at the kringle level. One of these mutations involves a trp72 to arg substitution in apo(a) kringle type 10 and is attended by a defective binding of Lp(a) to immobilized lysine/fibrin. Other mutations affecting the other amino acids of the "lysine-binding pocket" may have similar functional consequences and may be important at the clinical level in terms of thrombogenesis.
Lp(a)的大小多态性已得到充分认识。现在很明显，由于kringle水平发生的突变，还存在另一种多态性。其中一种突变涉及载脂蛋白(a)kringle 10型中色氨酸72被精氨酸取代，并且伴随着Lp(a)与固定化赖氨酸/纤维蛋白的结合缺陷。影响“赖氨酸结合口袋”其他氨基酸的其他突变可能具有类似的功能后果，并且在血栓形成方面在临床水平上可能很重要。
