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ECB-ART-34986
Biochem Biophys Res Commun 1984 Jun 15;1212:598-604. doi: 10.1016/0006-291x(84)90224-9.
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Purification and characterization of trypsin-like enzyme from sea urchin eggs: substrate specificity and physiological role.

Sawada H , Miura M , Yokosawa H , Ishii S .


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A trypsin-like enzyme has been purified to homogeneity from eggs of the sea urchin, Strongylocentrotus intermedius. The purified enzyme efficiently hydrolyzed Z-Phe-Arg-4- methylcoumaryl -7-amide (MCA) and Pro-Phe-Arg-MCA among 12 peptidyl-Arg (or Lys)- MCAs . The substrate specificity of the enzyme was closely similar to that of the enzyme activity in the egg cortical granule exudate. Among various peptidyl-argininal (Arg-H) derivatives, Z-Phe-Arg-H and Z-Phe-Leu-Arg-H showed the strongest inhibition against both the activity of the purified enzyme and the elevation of vitelline coat. Thus, the trypsin-like enzyme of sea urchin possesses a narrow substrate specificity and participates at least in the elevation of vitelline coat during fertilization.

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Genes referenced: LOC100887844