The exogastrula-inducing peptides in embryos of the sea urchin, Anthocidaris crassispina--isolation and determination of the primary structure. 1989

T Suyemitsu, and T Asami-Yoshizumi, and S Noguchi, and Y Tonegawa, and K Ishihara
Department of Regulation Biology, Faculty of Science, Saitama University, Japan.

Four exogastrula-inducing peptides, A, B, C, and D have been isolated from the homogenates of embryos of the sea urchin, Anthocidaris crassispina, with successive chromatographic fractionations. The complete amino acid sequences of the peptides A and D were determined by analysis of the peptides generated by their digestion with lysyl endopeptidase. They were composed of 52 and 53 amino acid residues, and their molecular weights were calculated to be 5754 and 5737, respectively. The sequences of peptides A and D were DSVYQCNRDTNSCDGFGKCEKSTFGRTTGQYICNCDDGYRNNAYGGCSPRTE, and DTVARCERDTKNCDGHGTCQLSTFGRRTGQYICFCDAGYRKPNSYGGCSPSSA, respectively. The biological significance of the exogastrula-inducing peptides was discussed.

UI MeSH Term Description Entries
D007447 Invertebrate Hormones Hormones produced by invertebrates, usually insects, mollusks, annelids, and helminths. Hormones, Invertebrate
D008297 Male Males
D008666 Metalloendopeptidases ENDOPEPTIDASES which use a metal such as ZINC in the catalytic mechanism. Metallo-Endoproteinases,Metalloendopeptidase
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D002851 Chromatography, High Pressure Liquid Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed. Chromatography, High Performance Liquid,Chromatography, High Speed Liquid,Chromatography, Liquid, High Pressure,HPLC,High Performance Liquid Chromatography,High-Performance Liquid Chromatography,UPLC,Ultra Performance Liquid Chromatography,Chromatography, High-Performance Liquid,High-Performance Liquid Chromatographies,Liquid Chromatography, High-Performance
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D005260 Female Females
D005775 Gastrula The developmental stage that follows BLASTULA or BLASTOCYST. It is characterized by the morphogenetic cell movements including invagination, ingression, and involution. Gastrulation begins with the formation of the PRIMITIVE STREAK, and ends with the formation of three GERM LAYERS, the body plan of the mature organism. Archenteron,Blastopore,Gastrocoele,Primitive Gut,Archenterons,Blastopores,Gastrocoeles,Gastrulas,Gut, Primitive,Guts, Primitive,Primitive Guts
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein

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