Dopheide T A, Ward C W
J Gen Virol. 1980 Oct;50(2):329-35. doi: 10.1099/0022-1317-50-2-329.
The amino acid sequence of the Hong Kong haemagglutinin light chang (HA2:222 residues) is nearly complete, lacking only the definition of a highly aggregated region near the carboxyl terminal end of the chain. This unsequenced area of approx. 25 residues occurs near the carboxyl terminal end of cyanogen bromide peptide CN-I, whose structure determination is discussed in this paper. All 1/2-cystine residues present in HA2 occur in CN-I, as a proximal cluster involving residues 137, 144 and 148, and as a distal cluster involving four other 1/2-cystine within peptides. The single glycosylated asparagine in HA2 also occurs in CN-I; the carbohydrates moiety is complex. The structure of HA2 is discussed in terms of its properties, and compared with published data from haemagglutinins from other influenza strains.
香港血凝素轻链（HA2：222个残基）的氨基酸序列几乎完整，仅缺少链羧基末端附近高度聚集区域的定义。这个约25个残基的未测序区域出现在溴化氰肽CN-I的羧基末端附近，本文讨论了其结构测定。HA2中存在的所有半胱氨酸残基都出现在CN-I中，形成一个近端簇，涉及残基137、144和148，以及一个远端簇，涉及肽内的其他四个半胱氨酸。HA2中唯一的糖基化天冬酰胺也出现在CN-I中；碳水化合物部分是复杂的。本文根据HA2的特性讨论了其结构，并与其他流感毒株血凝素的已发表数据进行了比较。
