TY - JOUR
T1 - Characterization of an anionic trypsin from the eel (anguilla japonica)
AU - Yoshinaka, Reiji
AU - Sato, Mamoru
AU - Suzuki, Tohru
AU - Ikeda, Shizunori
PY - 1985
Y1 - 1985
N2 - 1. 1. An enzyme, isolated from the pancreas of the eel Anguilla japonica and designated as anionic trypsin 1, had a molecular weight of 26,000 and an isoelectric point of 5.5. 2. 2. The amino acid composition of the enzyme was similar to that of bovine cationic trypsin as well as anionic trypsins from other species of fish. 3. 3. The enzyme was stable at pH 6 to 9 in the presence of calcium ions. 4. 4. Km and kcat values of the enzyme for N-tosyl-l-arginine methyl ester and N-tosyl-l-lysine methyl ester were quite similar to those of catfish anionic and bovine cationic trypsins.
AB - 1. 1. An enzyme, isolated from the pancreas of the eel Anguilla japonica and designated as anionic trypsin 1, had a molecular weight of 26,000 and an isoelectric point of 5.5. 2. 2. The amino acid composition of the enzyme was similar to that of bovine cationic trypsin as well as anionic trypsins from other species of fish. 3. 3. The enzyme was stable at pH 6 to 9 in the presence of calcium ions. 4. 4. Km and kcat values of the enzyme for N-tosyl-l-arginine methyl ester and N-tosyl-l-lysine methyl ester were quite similar to those of catfish anionic and bovine cationic trypsins.
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U2 - 10.1016/0305-0491(85)90415-8
DO - 10.1016/0305-0491(85)90415-8
M3 - Article
C2 - 3967484
AN - SCOPUS:0021983266
SN - 1096-4959
VL - 80
SP - 11
EP - 14
JO - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
JF - Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
IS - 1
ER -