Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z.
复制标题
DOI：
--
复制
发表时间：
1989-12
期刊：
影响因子：
--
通讯作者：
H. Nishimura;S. Kawabata;W. Kisiel;S. Hase;T. Ikenaka;T. Takao;Y. Shimonishi;S. Iwanaga
中科院分区：
文献类型：
--
作者：
H. Nishimura;S. Kawabata;W. Kisiel;S. Hase;T. Ikenaka;T. Takao;Y. Shimonishi;S. Iwanaga
我们最近描述了一种与牛血凝固因子 VII (Ser-52) 和 IX (Ser-53) 的第一个表皮生长因子样结构域中的丝氨酸残基相连的独特三糖（Hase, S.、Kawabata, S.、Nishimura, H.、Takeya, H.、Sueyoshi, T.、Miyata, T.、Iwanaga, S.、Takao, T.、Shimonishi, Y. 和Ikenaka, T. (1988) J. Biochem. (东京) 104, 867-868)。这些凝血因子中鉴定的糖链由 1 mol 己糖（葡萄糖 (Glc]）和 2 mol 戊糖（木糖 (Xyl]）组成。我们在此报告，人因子 VII 和 IX 以及蛋白 Z 和牛蛋白 Z 也包含与牛因子 VII 和 IX 中发现的相同位置处的丝氨酸残基连接的碳水化合物部分。对源自这些蛋白中的每一种的糖肽进行氨基酸序列和成分糖分析和快原子轰击质谱分析结果表明，来自人因子IX的糖肽含有1mol的Glc和Xyl。通过分析肼解产生的二糖，该二糖的还原端被鉴定为Glc。相比之下，人因子VII和蛋白质Z产生两种不同的糖肽，其摩尔比分别为1:1和1:2，表明这些O-连接糖的微观异质性。牛蛋白Z糖肽含有1mol Glc和2mol Xyl。通过对先前在牛因子VII和IX中发现的三糖糖链的分析证实了这些糖组成，这些发现表明除了牛蛋白Z之外，在人因子VII和IX以及蛋白Z的第一表皮生长因子样结构域中还存在Xyl2-Glc-Ser和Xyl-Glc-Ser结构。这些碳水化合物部分是否有助于这些蛋白质的生物活性尚不清楚。
We have recently described a unique trisaccharide linked to a serine residue in the first epidermal growth factor-like domains of bovine blood coagulation factors VII (Ser-52) and IX (Ser-53) (Hase, S., Kawabata, S., Nishimura, H., Takeya, H., Sueyoshi, T., Miyata, T., Iwanaga, S., Takao, T., Shimonishi, Y., and Ikenaka, T. (1988) J. Biochem. (Tokyo) 104, 867-868). The sugar chain identified in these clotting factors consists of 1 mol of hexose (glucose (Glc] and 2 mol of pentose (xylose (Xyl]. We report here that human factors VII and IX and protein Z and bovine protein Z also contain such carbohydrate moieties linked to a serine residue at the same position found in bovine factors VII and IX. A glycopeptide derived from each of these proteins was subjected to amino acid sequence and component sugar analyses and fast atom bombardment mass spectrometric analysis. The results indicate that the glycopeptide derived from human factor IX contains 1 mol each of Glc and Xyl. The reducing end of this disaccharide was identified as Glc by analyzing the disaccharide generated by hydrazinolysis. In contrast, human factor VII and protein Z yielded two different glycopeptides which contained Glc and Xyl at molar ratios of 1:1 and 1:2, respectively, suggesting microheterogeneity of these O-linked sugar chains. Bovine protein Z glycopeptide contained 1 mol of Glc and 2 mol of Xyl. These sugar compositions were confirmed by analyses of the intact proteins. In relation to the trisaccharide sugar chain previously discovered in bovine factors VII and IX, these findings indicate the existence of a Xyl2-Glc-Ser and a Xyl-Glc-Ser structure in the first epidermal growth factor-like domains of human factors VII and IX and protein Z in addition to that of bovine protein Z. Whether these carbohydrate moieties contribute to the biological activities of these proteins is unknown.