Christomanou H, Kleinschmidt T, Braunitzer G
Max-Planck-Institut für Psychiatrie, München.
Biol Chem Hoppe Seyler. 1987 Sep;368(9):1193-6. doi: 10.1515/bchm3.1987.368.2.1193.
A naturally occurring non-enzymic sphingolipid activator protein (A1a activator) shown previously to be immunochemically not detectable in a new variant of human Gaucher disease (glucosylceramide-lipidosis) without glucosylceramidase deficiency was characterized by partial sequence analysis. The N-terminal amino-acid sequence of the A1a activator--a glycoprotein with high carbohydrate content--could be determined up to position 38. About 20% of the polypeptide chain are shorter by two amino-acid residues at the N-terminal end. Position 22 seems to be occupied by a carbohydrate-binding asparagine. The N-terminus of the A1a activator does not show any homology with the activator for the enzymic sulfatide degradation.
先前已证明，在一种新的人类戈谢病（葡糖脑苷脂贮积症）变体中，尽管不存在葡糖脑苷脂酶缺乏，但天然存在的非酶鞘脂激活蛋白（A1a激活剂）在免疫化学上无法检测到，现通过部分序列分析对其进行了表征。A1a激活剂是一种碳水化合物含量高的糖蛋白，其N端氨基酸序列可确定到第38位。约20%的多肽链在N端缩短了两个氨基酸残基。第22位似乎被一个碳水化合物结合天冬酰胺占据。A1a激活剂的N端与酶促硫脂降解的激活剂没有任何同源性。
