title: Purification of EGIP-D-binding protein from the embryos of the sea urchin Anthocidaris crassispina.
abstract: 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.
authors.affiliation: Department of Regulation Biology, Faculty of Science, Saitama University, Urawa, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Fujita
authors.forename: Y
authors.initials: Y
authors.lastname: Hirate
authors.forename: T
authors.initials: T
authors.lastname: Hiyama
authors.forename: K
authors.initials: K
authors.lastname: Yamasu
authors.forename: T
authors.initials: T
authors.lastname: Suyemitsu
authors.forename: K
authors.initials: K
authors.lastname: Ishihara
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004625:Embryo, Nonmammalian / Q000378:metabolism*; D007447:Invertebrate Hormones / Q000378:metabolism*; D008969:Molecular Sequence Data; D018010:Receptors, Invertebrate Peptide / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D012617:Sea Urchins / Q000196:embryology*; D017386:Sequence Homology, Amino Acid
chemical_list: C111344:EGIP-D-binding protein, Anthocidaris crassispina; D007447:Invertebrate Hormones; D018010:Receptors, Invertebrate Peptide; C061709:exogastrula-inducing peptide D, Anthocidaris crassispina