When dialyzed extracts from hake (Merluccius hubbsi) skeletal muscle were chromatographed in DEAE-Sephacel, an alkaline protease (37 degrees C, pH 8.5) and a trypsin inhibitor were isolated. The enzyme showed its maximal activity against azocasein in the range of pH between 7 and 9. The ...
1). Furthermore the vertebrate acrosins, found in sperm cells, form a distinct group within a well-supported monophyletic clade that includes Cortex Granule Serine Protease 1 (CGSP1) found in sea urchin eggs. Most of the internal nodes in the phylogenetic tree were not supported (Fig. 1) ...
An alkaline serineprotease, capable of hydrolyzing - grown in the presence of gelatin as the sole nitrogen and carbon source. The protease was purified 65-fold to electrophoretic homogenity from the culture supernatant in a three-step procedure comprising QSepharose chromatography, affinity ...
Trypsin activity increases at alkaline pH, with optimal pH ranging from 7 to 10 [39]. With the fact that the temperature and pH were insufficient to induce inactivation of the enzyme, thus their effect can be neglected. Table 3. Effect of ACP on pH of purified trypsin at different ...