The primary structure of chicken muscle acylphosphatase isozyme Ch2 |
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Authors: | Y Ohba O Minowa Y Mizuno H Shiokawa |
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Affiliation: | Institute of Immunological Science, Hokkaido University. |
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Abstract: | The amino acid sequence of one, Ch2, of the two isozymes of chicken muscle acylphosphatase was determined. It consists of 98 amino acid residues with N-acetylalanine at the amino(N)-terminus and contains no cysteine: Ac-Ala-Gly-Ser-Glu- Gly-Leu-Met-Ser-Val-Asp-Tyr-Glu-Val-Ser-Gly-Arg-Val-Gln-Gly-Val-Phe-Phe- Arg- Lys-Tyr-Thr-Gln-Ser-Glu-Ala-Lys-Arg-Leu-Gly-Leu-Val-Gly-Trp-Val-Arg-Asn- Thr- Ser-His-Gly-Thr-Val-Gln-Gly-Gln-Ala-Gln-Gly-Pro-Ala-Ala-Arg-Val-Arg-Glu- Leu- Gln-Glu-Trp-Leu-Arg-Lys-Ile-Gly-Ser-Pro-Gln-Ser-Arg-Ile-Ser-Arg-Ala-Glu- Phe- Thr-Asn-Glu-Lys-Glu-Ile-Ala-Ala-Leu-Glu-His-Thr-Asp-Phe-Gln-Ile-Arg-Lys- COOH. The sequence differs in 44% of the total positions from the other isozyme, Ch1. Comparison of the sequence and the predicted conformational profile of Ch2 with those of Ch1 suggests that they share a common evolutionary origin and appear to have retained similar conformations throughout their evolutionary development. |
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