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. 1986 Aug;83(16):5840–5843. doi: 10.1073/pnas.83.16.5840

Amino acid sequence of a prothoracicotropic hormone of the silkworm Bombyx mori

Hiromichi Nagasawa *, Hiroshi Kataoka *, Akira Isogai *, Saburo Tamura *, Akinori Suzuki *, Akira Mizoguchi †, Yuko Fujiwara †, Atsushi Suzuki †, Susumu Y Takahashi †, Hironori Ishizaki †
PMCID: PMC386391  PMID: 16593744

Abstract

We have determined the complete amino acid sequence of 4K-PTTH-II, one of three forms of the Mr 4400 prothoracicotropic hormone of the silkworm Bombyx mori, active to brainless pupae of Samia cynthia ricini. Like vertebrate insulin, it consists of two nonidentical peptide chains (A and B chains). The A chain consists of 20 amino acid residues. The B chain is a mixture of four microheterogeneous peptides, two of which consist of 28 residues, and the other two, of 26 residues. 4K-PTTH-II has considerable sequence homology (40%) with human insulin, and it resembles porcine relaxin both in the carboxyl-terminal cysteine residue of the A chain and in the amino-terminal pyroglutamic acid residue of the B chain. The identical distribution of the six cysteine residues also indicates that 4K-PTTH-II belongs to the insulin family.

Keywords: insulin, relaxin

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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