人黏液分泌物的酸稳定蛋白酶抑制剂（HUSI-I，抗白细胞蛋白酶）。通过蛋白质和cDNA测序揭示的完整氨基酸序列以及与乳清蛋白和红海龟蛋白酶抑制剂的结构同源性。
The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease). Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red Sea turtle proteinase inhibitor.
作者信息
Seemüller U, Arnhold M, Fritz H, Wiedenmann K, Machleidt W, Heinzel R, Appelhans H, Gassen H G, Lottspeich F
出版信息
FEBS Lett. 1986 Apr 7;199(1):43-8. doi: 10.1016/0014-5793(86)81220-0.
The complete amino acid sequence of human antileukoprotease has been determined by direct sequencing of the inhibitory active protein isolated from seminal plasma (HUSI-I) and by sequence analysis of cDNA reverse-transcribed from mRNA prepared from cervical tissue. The inhibitor (Mr 11726) consists of 107 amino acid residues including 16 cysteines presumably forming disulfide bonds. The molecule comprises two consecutive domains which are homologous to each other, to the second domain of the basic protease inhibitor from Red Sea turtle (chelonianin) and to both domains of the whey proteins of rat and mouse. Both domains contain a pattern of cysteines known as the 'four-disulfide-core' that has also been found in wheat germ agglutinin and neurophysin.
人抗白细胞蛋白酶的完整氨基酸序列已通过对从精浆中分离出的抑制活性蛋白（HUSI-I）进行直接测序以及对从宫颈组织制备的mRNA反转录得到的cDNA进行序列分析得以确定。该抑制剂（Mr 11726）由107个氨基酸残基组成，包括16个可能形成二硫键的半胱氨酸。该分子包含两个连续的结构域，这两个结构域彼此同源，与红海龟碱性蛋白酶抑制剂（chelonianin）的第二个结构域同源，也与大鼠和小鼠乳清蛋白的两个结构域同源。两个结构域都含有一种被称为“四二硫键核心”的半胱氨酸模式，这种模式也在麦胚凝集素和神经垂体素中被发现。
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