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   <subfield code="a">Purification and Characterization of Turtle Pepsinogen and Pepsin</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[Akira Hirasawa, Senarath B.P. Athauda, Kenji Takahashi]</subfield>
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   <subfield code="a">Pepsinogen was purified from the gastric mucosa of soft-shelled turtle (Trwnyx sinensis) by a series of chromatographies on DEAE-cellulose, Sephadex G-100, and Q-Sepharose. Upon chromatography on Q-Sepharose, it was separated into nine isoforms. These isoforms showed a relative molecular mass of approximately 43,000 Da on sodium dodecyl sulfatepolyacrylamide gel electrophoresis, and isoforms 4 through 9 contained carbohydrate (approx. 2% each). Insofar as they were examined, their NH2-terminal sequences differed only in showing substitution at a few positions. At pH 2.0, they were rapidly activated to the corresponding isoforms of pepsin in a stepwise manner. The nine isoforms showed similar specific activity toward hemoglobin and hydrolyzed N-acetyl-L-phenylalanyl- L-diiodotyrosine, a good substrate for pepsin A, at somewhat different rates. They were inhibited by pepstatin to various extents, more strongly than human pepsin C but less strongly than human pepsin A. All isoforms appeared to have similar cleavage specificity toward oxidized insulin B chain, which resembled those of both human pepsins A and C. A cDNA clone for one of the zymogen isoforms was isolated and sequenced. The amino acid sequence thus deduced was more homologous with those of mammalian pepsinogens A than those of mammalian pepsinogens C or prochymoain.</subfield>
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   <subfield code="a">© 1996 BY THE JOURNAL OF BIOCHEMISTRY</subfield>
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   <subfield code="a">amino acid sequence</subfield>
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