Author:
Stevenson Kenneth J.,Gibson David,Dixon Gordon H.
Abstract
Amino acid analyses of two chymotrypsin-like serine proteases (designated proteases A and B) isolated from the gastric tissue of the sea anemone (Metridium senile) were conducted. Proteases A and B are distinct enzymes and are not related by minor proteolytic digestion. These enzymes contain similar total amino acid compositions of about 240 residues. The findings in protease A of a very high proline content (30 residues) and six residues of an unique amino acid, 2-aminoethylphosphonic acid (2-AEP; H2NCH2CH2PO3H), are of interest. 2-AEP was characterized on the amino acid analyzer and on high-voltage ionophoresis at pH 6.5. In protease B, four residues of 2-AEP were present and an anomaly was observed with the arginine residues.
Publisher
Canadian Science Publishing
Cited by
9 articles.
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