Powell J R, Castellino F J
Biochemistry. 1983 Feb 15;22(4):923-7. doi: 10.1021/bi00273a033.
The amino acid sequences of the two major carbohydrate variants in the region of Asn288 have been determined. A peptide isolated from plasminogen variant 1, which contains a complex-type Asn288-linked oligosaccharide, was found to possess the amino acid sequence-Ser280-Ala-Gln-Thr-Pro-His-Thr-His-Asn(CHO)-Arg-Thr290-Pro-Glu-, in agreement with the previously published sequence [Sottrup-Jensen, L., Claeys, H., Zajdel, M., Petersen, T. E., & Magnusson, S. (1978) in Progress in Chemical Fibrinolysis and Thrombolysis (Davidson, J. F., Rowan, R. M., Samama, M. M., & Desnoyers, P. C., Eds.) Vol. 3, pp 191-209, Raven Press, New York]. A similar peptide isolated from plasminogen variant 2 did not contain oligosaccharide but possessed an amino acid sequence identical with the corresponding variant 1 peptide. Thus, the basis for the lack of the complex-type oligosaccharide in human plasminogen variant 2 does not reside in substitution of essential amino acid residues in the region of the Asn288-linked glycosylation site.
已确定了Asn288区域中两种主要碳水化合物变体的氨基酸序列。从纤溶酶原变体1中分离出的一种肽，其含有一个复合型Asn288连接的寡糖，被发现具有氨基酸序列-Ser280-Ala-Gln-Thr-Pro-His-Thr-His-Asn(CHO)-Arg-Thr290-Pro-Glu-，这与先前发表的序列一致[Sottrup-Jensen, L., Claeys, H., Zajdel, M., Petersen, T. E., & Magnusson, S. (1978) in Progress in Chemical Fibrinolysis and Thrombolysis (Davidson, J. F., Rowan, R. M., Samama, M. M., & Desnoyers, P. C., Eds.) Vol. 3, pp 191 - 209, Raven Press, New York]。从纤溶酶原变体2中分离出的一种类似肽不含寡糖，但具有与相应的变体1肽相同的氨基酸序列。因此，人纤溶酶原变体2中缺乏复合型寡糖的原因并不在于Asn288连接的糖基化位点区域中必需氨基酸残基的取代。
