Document Detail

The complete amino acid sequence of echinoidin, a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina. Homologies with mammalian and insect lectins.
MedLine Citation:
PMID:  3571253     Owner:  NLM     Status:  MEDLINE    
The complete amino acid sequence of echinoidin, the proposed name for a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina, has been determined by sequencing the peptides obtained from tryptic, Staphylococcus aureus V8 protease, chymotryptic, and thermolysin digestions. Echinoidin is a multimeric protein (Giga, Y., Sutoh, K., and Ikai, A. (1985) Biochemistry 24, 4461-4467) whose subunit consists of a total of 147 amino acid residues and one carbohydrate chain attached to Ser38. The molecular weight of the polypeptide without carbohydrate was calculated to be 16,671. Each polypeptide chain contains seven half-cystines, and six of them form three disulfide bonds in the single polypeptide chain (Cys3-Cys14, Cys31-Cys141, and Cys116-Cys132), while Cys2 is involved in an interpolypeptide disulfide linkage. From secondary structure prediction by the method of Chou and Fasman (Chou, P. Y., and Fasman, G. D. (1974) Biochemistry 13, 211-222) the protein appears to be rich in beta-sheet and beta-turn structures and poor in alpha-helical structure. The sequence of the COOH-terminal half of echinoidin is highly homologous to those of the COOH-terminal carbohydrate recognition portions of rat liver mannose-binding protein and several other hepatic lectins. This COOH-terminal region of echinoidin is also homologous to the central portion of the lectin from the flesh fly Sarcophaga peregrina. Moreover, echinoidin contains an Arg-Gly-Asp sequence which has been proposed to be a basic functional unit in cellular recognition proteins.
Y Giga; A Ikai; K Takahashi
Related Documents :
7104373 - Circular dichroism studies on the proline-rich glycoprotein of human parotid saliva.
10626373 - An isolectin complex from trichosanthes anguina seeds.
1778303 - Primary structure and tissue distribution of anglerfish carboxypeptidase h.
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  262     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1987 May 
Date Detail:
Created Date:  1987-06-05     Completed Date:  1987-06-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  6197-203     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Lectins / analysis*
Sea Urchins
Reg. No./Substance:
0/Lectins; 110279-94-2/echinoidin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Upper and lower limits of the charge translocation stoichiometry of mitochondrial electron transport...
Next Document:  Mitochondrial DNA displacement loop structure depends on growth state in bovine cells.