A Protease Inhibitor of the Serpin Family Is a Major Protein in Carp Perimeningeal Fluid: I. Protein Purification and Characterization
Resource
Journal of Neurochemistry 64 (4): 1715-1720
Journal
Journal of Neurochemistry
Pages
1715-1720
Date Issued
1995
Date
1995
Author(s)
Abstract
Abstract: 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 α1‐antitrypsin in many aspects, it is likely a fish equivalent of α1‐antitrypsin. Copyright © 1995, Wiley Blackwell. All rights reserved
Subjects
Perimeningeal fluid; Protease inhibitor; Serine protease; Serpin
Other Subjects
alpha 1 antitrypsin; proteinase inhibitor; serine proteinase; serine proteinase inhibitor; animal tissue; article; brain; carp; cerebrospinal fluid; controlled study; hypophysis; kidney; liver; muscle; nonhuman; ovary; priority journal; protein determination; protein localization; protein purification; proteinase inhibition; spleen; tissue distribution; Animal; Body Fluids; Carps; Cattle; Chymotrypsin; Glycoside Hydrolases; Glycosylation; Isoenzymes; Meninges; Molecular Weight; Nerve Tissue Proteins; Pancreatic Elastase; Protease Inhibitors; Serpins; Support, Non-U.S. Gov't; Swine; Tissue Distribution; Trypsin Inhibitors
Type
journal article
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