Identification of a novel type of processing sites in the precursor for the sea anemone neuropeptide Antho-RFamide (<Glu-Gly-Arg-Phe-NH2) from Anthopleura elegantissima.
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چکیده
منابع مشابه
Characterization of a novel EF-hand homologue, CnidEF, in the sea anemone Anthopleura elegantissima.
The superfamily of EF-hand proteins is comprised of a large and diverse group of proteins that contain one or more characteristic EF-hand calcium-binding domains. This study describes and characterizes a novel EF-hand cDNA, CnidEF, from the sea anemone Anthopleura elegantissima (Phylum Cnidaria, Class Anthozoa). CnidEF was found to contain two EF-hand motifs near the C-terminus of the deduced a...
متن کاملThe expansion behaviour of sea anemones may be coordinated by two inhibitory neuropeptides, Antho-KAamide and Antho-RIamide.
Antho-KAamide (L-3-phenyllactyl-Phe-Lys-Ala-NH2) and Antho-RIamide (L-3-phenyllactyl-Tyr-Arg-Ile-NH2) are novel neuropeptides isolated from the sea anemone Anthopleura elegantissima. They both inhibited spontaneous contractions of isolated muscle preparations from a wide variety of anemone species (threshold around 10(-7) M). Their actions were universal in that they inhibited every muscle prep...
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The expansion behaviour of sea anemones may be coordinated by two inhibitory neuropeptides, Antho-KAamide and Antho-RIamide
Antho-KAamide (L-3-phenyllactyl-Phe-Lys-Ala-NH2) and Antho-RIamide (L-3-phenyllactyl-Tyr-ArgIle-NH2) are novel neuropeptides isolated from the sea anemone Anthopleura elegantissima. They both inhibited spontaneous contractions of isolated muscle preparations from a wide variety of anemone species (threshold around 1CT7 m). Their actions were universal in that they inhibited every muscle prepara...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1992
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)41705-x