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• W2017293136 abstract "Anionic trypsin from Pacific saury (Cololabis saira) pyloric ceca was purified to homogeneity by ammonium sulfate precipitation, ion-exchange chromatography, and gel filtration chromatography. It was purified to 53.7-fold with a yield of 6.1%. The apparent molecular weight of the enzyme was about 24 kDa, as determined by size exclusion chromatography and sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). On native-PAGE, trypsin showed a single band. The purified anionic trypsin displayed optimal activity at pH 8.5 and 55°C. The enzyme was stable at neutral and alkaline pH and in the temperature range of 20–50°C. The stability was affected by the calcium ion. The activity of purified anionic trypsin was completely inhibited by soybean trypsin inhibitor and N-p-tosyl-L-lysine chloromethyl ketone (TLCK) and partially inhibited by ethylenediaminetetraacetic acid (EDTA). NaCl (0–30%) decreased the activity in a concentration-dependent manner. The kinetic trypsin constants Km and Kcat were 0.19 mM and 210 s−1, respectively, while the catalytic efficiency (Kcat/Km) was 1105.26 s−1 mM−1. The N-terminal amino acid sequences of anionic trypsin, IVGGYECQAH, were found and were homologous to those of trypsin from other fish species." @default.
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• W2017293136 date "2014-01-27" @default.
• W2017293136 modified "2023-10-05" @default.
• W2017293136 title "Anionic Trypsin from the Pyloric Ceca of Pacific Saury (<i>Cololabis saira</i>): Purification and Biochemical Characteristics" @default.
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• W2017293136 doi "https://doi.org/10.1080/10498850.2012.708387" @default.
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