Some Aspects of the Relationship between N-Terminal Structure and MSH Activity of Three Decapeptides Related to ACTH : A Comparative Study of Gly<SUP>1</SUP>-ACTH (1-10) OH, Ibu<SUP>1</SUP>-ACTH (1-10) OH and β-Ala<SUP>1</SUP>-ACTH (1-10) OH

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概要

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• <I>In vivo</I> MSH activities of three decapeptides, Gly<SUP>1</SUP>-ACTH (1-10) OH, Ibu<SUP>1</SUP>-ACTH (1-10) OH, β-Ala<SUP>1</SUP>-ACTH (1-10) OH, and a tetradecapeptide Gly<SUP>1</SUP>-ACTH (1-14) OH were compared with those of three octadecapeptides having N-terminal amino acid residues common to the respective shorter peptides; Gly<SUP>1</SUP>-ACTH (1-18) NH<SUB>2</SUB>, ACTH (1-18) NH2, and β-Ala<SUP>1</SUP>-ACTH-(1-18) NH<SUB>2</SUB>. The three decapeptides had almost the same minimum effective dose in assays in African frog, <I>Xenopus laevis D.</I> The potencies of three decapeptides were about 1/1, 000 of the potency of α-MSH on a weight basis and the tetradecapeptide was 1/640. The octadecapeptides, however, showed differing MSH potencies: Glyi-ACTH (1-18) NI12 was 1/48 as potent as α-MSH;β-Ala<SUP>1</SUP>-ACTH (1-18) NH<SUB>2</SUB> and Ibu<SUP>1</SUP>-ACTH (1-18) NH<SUB>2</SUB> exhibited 1/1.5-1/2.5 of the potency of α-MSH respectively. A possible mechanism explaining why the effect of substitution of the Nterminal residue on MSH activity is different in decapeptides and octadecapeptides is considered.

• 社団法人 日本内分泌学会の論文

著者

• TANAKA AKIRA

  Shionogi Research Laboratory, Shionogi Co. Ltd.

• Nakamura Masuhisa

  Shionogi Research Laboratories Shionogi & Co. Ltd.

• NAKAMURA MASUHISA

  Shionogi Research Laboratory

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