| Budget Amount *help |
¥2,100,000 (Direct Cost: ¥2,100,000)
Fiscal Year 1987: ¥700,000 (Direct Cost: ¥700,000)
Fiscal Year 1986: ¥1,400,000 (Direct Cost: ¥1,400,000)
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| Research Abstract |
To elucidate the biological roles on N-acylamino acid releasing-enzyme, its substrate specificity was at first studied with acetylmethionyl amino acids, acetylalanyl peptides ranging from dithrough penta-alanine, and N-acylmethionylalanine having various acyl groups, and the following results were thus found. 1) The enzyme hydrolyses all the peptides tested except for acetyl-L-methionuyl-L-proline, -L-aspartic acid and -D-amino acids. 2) Among acetylated derivatives of oligoalanine, acetyl di- and trialanine were most rapidly hydrolyzed by the enzyme. 3) The enzyme removes more effectively acetyl or propionyl amino acid from various N-acylated peptides. As the second step, the determination of the primary structure of the enzyme was tried. Amino acid sequences of several peptides generated from the enzyme from pig liver, by digestion with Achromobacter protease I were partially determined, and the isolation of cDNA encoding the enzyme has been now performing in the cDNA library constructed from pig liver using a 24-mer nucleotide corresponding to the sequence partially determined as above, Glu-Pro-Glu-Glu-Ala-Ala-Ala-Leu-Tyr, as a prove.
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