Determination of the amino acid sequence of the moult-inhibiting hormone from the edible crab, Cancer pagurus

J. S. Chung; Mark Wilkinson; S. G. Webster

doi:10.1016/s0143-4179(96)90061-x

Determination of the amino acid sequence of the moult-inhibiting hormone from the edible crab, Cancer pagurus

J. S. Chung, Mark Wilkinson, S. G. Webster

Research output: Contribution to journal › Article › peer-review

42 Citations (Scopus)

Abstract

Putative moult-inhibiting hormone (MIH) from sinus glands of the edible crab Cancer pagurus was characterized by high-performance liquid chromatography, followed by fractional bioassay (inhibition of ecdysteroid synthesis by Y-organs) and immunoassay (using antisera raised against Carcinus MIH). This peptide was fully sequenced by automated Edman degradation of endoproteinase-derived fragments. C, pagurus MIH is a 78 residue peptide (M(r) 9194), with free N- and C-termini and three intrachain disulphide bridges. Comparison with previously published MIH sequences confirms a high degree of sequence identity (c. 80%), supporting the view that brachyurans (crabs), possess distinct, structurally similar MIH neuropeptides.

Original language	English
Pages (from-to)	95-101
Number of pages	7
Journal	Neuropeptides
Volume	30
Issue number	1
DOIs	https://doi.org/10.1016/s0143-4179(96)90061-x
Publication status	Published - 1 Jan 1996
Externally published	Yes

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title = "Determination of the amino acid sequence of the moult-inhibiting hormone from the edible crab, Cancer pagurus",

abstract = "Putative moult-inhibiting hormone (MIH) from sinus glands of the edible crab Cancer pagurus was characterized by high-performance liquid chromatography, followed by fractional bioassay (inhibition of ecdysteroid synthesis by Y-organs) and immunoassay (using antisera raised against Carcinus MIH). This peptide was fully sequenced by automated Edman degradation of endoproteinase-derived fragments. C, pagurus MIH is a 78 residue peptide (M(r) 9194), with free N- and C-termini and three intrachain disulphide bridges. Comparison with previously published MIH sequences confirms a high degree of sequence identity (c. 80\%), supporting the view that brachyurans (crabs), possess distinct, structurally similar MIH neuropeptides.",

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AU - Chung, J. S.

AU - Wilkinson, Mark

AU - Webster, S. G.

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AB - Putative moult-inhibiting hormone (MIH) from sinus glands of the edible crab Cancer pagurus was characterized by high-performance liquid chromatography, followed by fractional bioassay (inhibition of ecdysteroid synthesis by Y-organs) and immunoassay (using antisera raised against Carcinus MIH). This peptide was fully sequenced by automated Edman degradation of endoproteinase-derived fragments. C, pagurus MIH is a 78 residue peptide (M(r) 9194), with free N- and C-termini and three intrachain disulphide bridges. Comparison with previously published MIH sequences confirms a high degree of sequence identity (c. 80%), supporting the view that brachyurans (crabs), possess distinct, structurally similar MIH neuropeptides.

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EP - 101

JO - Neuropeptides

JF - Neuropeptides

IS - 1

ER -

Determination of the amino acid sequence of the moult-inhibiting hormone from the edible crab, Cancer pagurus

Abstract

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