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cDNA and deduced amino acid sequence of human PK‐120, a plasma kallikrein‐sensitive glycoprotein
Author(s) -
Hitoshi Nishimura,
Ikuko Kakizaki,
Tsuyoshi Muta,
Naosuke Sasaki,
Ping Xiao Pu,
Toshiyuki Yamashita,
Shigeharu Nagasawa
Publication year - 1995
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(94)01364-7
Subject(s) - kallikrein , peptide sequence , complementary dna , peptide , chemistry , trypsin , glycoprotein , amino acid , biochemistry , microbiology and biotechnology , human plasma , cleavage (geology) , biology , enzyme , gene , chromatography , paleontology , fracture (geology)
PK‐120 is a substrate for plasma kallikrein (PK), recently purified from human plasma. Here we have established the cDNA sequence for human PK‐120 mRNA. The deduced amino sequence of PK‐120 revealed that it consists of 902 amino acid residues with a calculated mass of 116,423 Da. The putative cleavage sites by PK have been proposed, suggesting that PK‐120 may be a precursor of a bioactive peptide. Most interestingly, PK‐120 showed significant sequence identities to heavy chains (HCs) of the inter‐α‐trypsin inhibitor (ITI) superfamily.