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The acid‐stable proteinase inhibitor of human mucous secretions (HUSI‐I, antileukoprotease)
Author(s) -
Seemüller Ursula,
Arnhold Marianne,
Fritz Hans,
Wiedenmann Karin,
Machleidt Werner,
Heinzel Regina,
Appelhans Heribert,
Gassen Hans-Günter,
Lottspeich Friedrich
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81220-0
Subject(s) - peptide sequence , biochemistry , complementary dna , protease inhibitor (pharmacology) , amino acid , chemistry , biology , microbiology and biotechnology , agglutinin , gene , lectin , genetics , virus , viral load , antiretroviral therapy
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 ( M r 11 726) 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.