Amino acid sequence of exogastrula-inducing peptide C from the sea urchin, Anthocidaris crassispina

• Published in: Biochimica et biophysica acta Vol. 999; no. 1; pp. 24 - 28
• Main Authors: Suyemitsu, Takashi, Tonegawa, Yasuto, Ishihara, Katsutoshi
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 09.11.1989; Elsevier; North-Holland
• Subjects: Amino Acid Sequence; amino acids; Amino Acids - analysis; Aminoacids, peptides. Hormones. Neuropeptides; Analytical, structural and metabolic biochemistry; Animals; Anthocidaris crassispina; Biological and medical sciences; biological development; Fundamental and applied biological sciences. Psychology; gastrulation; Invertebrate Hormones - metabolism; Marine; Molecular Sequence Data; Molecular Weight; Peptide Fragments - analysis; Peptide Fragments - metabolism; Proteins; Sea Urchins - embryology; Serine Endopeptidases - metabolism; ultrastructure; Embryonic development; Echinodermata; Induction; Homology; Echinoidea; Invertebrata; Sea urchin; C-Peptide; Aminoacid sequence
• ISSN: 0167-4838; 0006-3002; 1879-2588; 1878-2434
• DOI: 10.1016/0167-4838(89)90024-1

The complete amino acid sequence of exogastrula-inducing peptide C from embryos of the sea urchin, Anthocidaris crassipina has been determined by analysis of the amino acid sequences in the S-pyridylethylated peptide C and the peptides generated after digestion of the peptide C with arginyl endopeptidase. Exogastrula-inducing peptide C was composed of 58 amino acid residues and its molecular weight was calculated to be 6464. The sequence was DTKGGCERATNNCNGHGDCVQGRWGQYYCKCTLPYRVGGSESSCYMPKDKEEDVEIET.