Purification of EGIP-D-Binding Protein from the Embryos of the Sea Urchin Anthocidaris crassispina

• Published in: Zoological Science Vol. 14; no. 6; pp. 931 - 934
• Main Authors: Fujita, Yoshiaki, Hirate, Yoshikazu, Hiyama, Tetsuo, Yamasu, Kyo, Suyemitsu, Takashi, Ishihara, Katsutoshi
• Format: Journal Article
• Language: English
• Published: Japan Zoological Society of Japan 01.12.1997; UniBio Press
• Subjects: Amino Acid Sequence; Animals; Anthocidaris crassispina; Biotechnology; Electrophoresis, Polyacrylamide Gel; Embryo, Nonmammalian - metabolism; Invertebrate Hormones - metabolism; Marine; Molecular Sequence Data; Original s; Receptors, Invertebrate Peptide - chemistry; Receptors, Invertebrate Peptide - isolation & purification; Receptors, Invertebrate Peptide - metabolism; Sea Urchins - embryology; Sequence Homology, Amino Acid
• ISSN: 0289-0003
• DOI: 10.2108/zsj.14.931

Exogastrula-inducing peptides (EGIPs) are intrinsic factors that are present in eggs and embryos of the sea urchin Anthocidaris crassispina. They induce exogastrulation when added exogenously to the embryos. In the present study, we isolated an EGIP-D-binding protein (EBP) from a homogenate of mesenchyme blastulae. EBP had an apparent molecular weight of 33,000. The N-terminal amino acid sequence of EBP had a sequence homology to HLC-32 and bep4 identified in other sea urchin embryos. In addition to its ability of binding to EGIP-D, EBP also inhibited exogastrulation induced by EGIP-D. These results suggest that EBP plays an essential role in EGIP-D-induced exogastrulation.