Purification and Characterization of Serum Serpin from Carp (Cyprinus carpio) |
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Authors: | Futoshi Aranishi |
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Institution: | (1) Division of Physiology and Molecular Biology, National Research Institute of Fisheries Science, Yokohama 236-8648, Japan, JP |
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Abstract: | A serine proteinase inhibitor, termed serpin62, was purified to homogeneity from carp serum with an increase in specific
inhibitory activity of 6.2-fold and a 3% recovery rate after separation from α1-antitrypsin. Specific inhibitory activity of serpin62 against bovine pancreatic trypsin was less than half of the specific
antitryptic activity of α1-antitrypsin. Under both reducing and nonreducing conditions, serpin62 was estimated to have a molecular weight (62,000) apparently
larger than that of α1-antitrypsin (55,000). They both consist of single polypeptide chains, but serpin62 differs from serine proteinase inhibitors
from muscles of carp and white croaker in molecular weight and structure. Antibody raised against serpin62 immunologically
crossreacted with serpin62 and had no crossreactivity with fish serum α1-antitrypsin and muscular analogues. The antibody was susceptible to both serpin62 and its derivatives, which were widely
distributed in carp tissues. Serpin62 is most likely distinct from other fish serine proteinase inhibitors expressing antitryptic
activity physicochemically and immunologically.
Received June 4, 1998; accepted September 10, 1998. |
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Keywords: | : serine proteinase inhibitor serum serpin carp |
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