Premium
A Protease Inhibitor of the Serpin Family Is a Major Protein in Carp Perimeningeal Fluid: I. Protein Purification and Characterization
Author(s) -
Huang ChangJen,
Chen ChienChang,
Chen HsiuJane,
Huang ForeLien,
Chang GeenDong
Publication year - 1995
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1995.64041715.x
Subject(s) - biochemistry , protease , protease inhibitor (pharmacology) , serine protease , serpin , kunitz sti protease inhibitor , proteases , sodium dodecyl sulfate , glycoprotein , microbiology and biotechnology , biology , chymotrypsin , glycosylation , chemistry , trypsin , enzyme , human immunodeficiency virus (hiv) , viral load , antiretroviral therapy , gene , immunology
Two isoforms of a protease inhibitor of the serpin family (p62) have been purified from bighead carp perimeningeal fluid. Both isoforms migrate with an apparent molecular mass of 62 kDa on reducing and nonreducing sodium dodecyl sulfate‐polyacrylamide gels. Both proteins inhibited the activities of bovine trypsin, bovine chymotrypsin, and porcine pancreatic elastase. They also formed complexes with these proteases that were resistant to sodium dodecyl sulfate treatment. p62 exists in the extracts of all tissues examined, including brain, head kidney, kidney, liver, muscle, ovary, pituitary, and spleen. It is also present in serum, ovarian fluid, and milt as well as perimeningeal fluid. The protease inhibitor is a glycoprotein, and its carbohydrate moiety could be removed by endoglycosidase F. Because p62 resembles mammalian α 1 ‐antitrypsin in many aspects, it is likely a fish equivalent of α 1 ‐antitrypsin.