PURIFICATION OF EGIP-D-BINDING PROTEIN FROM THE EMBRYOS OF THE SEA-URCHIN ANTHOCIDARIS-CRASSISPINA

Citation
Y. Fujita et al., PURIFICATION OF EGIP-D-BINDING PROTEIN FROM THE EMBRYOS OF THE SEA-URCHIN ANTHOCIDARIS-CRASSISPINA, Zoological science, 14(6), 1997, pp. 931-934
Citations number
17
Journal title
ISSN journal
02890003
Volume
14
Issue
6
Year of publication
1997
Pages
931 - 934
Database
ISI
SICI code
0289-0003(1997)14:6<931:POEPFT>2.0.ZU;2-D
Abstract
Exogastrula-inducing peptides (EGIPs) are intrinsic factors that are p resent 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 wei ght of 33,000. The N-terminal amino acid sequence of EBP had a sequenc e 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 ex ogastrulation induced by EGIP-D. These results suggest that EBP plays an essential role in EGIP-D-induced exogastrulation.