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Titolo:
ISOLATION OF A CALCIUM-BINDING PHOSPHOPROTEIN FROM THE OOCYTES AND HEMOLYMPH OF THE BLOODSUCKING INSECT RHODNIUS-PROLIXUS
Autore:
SILVANETO MAC; ATELLA GC; FIALHO E; PAES MC; ZINGALI RB; PETRETSKI JH; ALVES EW; MASUDA H;
Indirizzi:
FED UNIV RIO DE JANEIRO,INST CIENCIAS BIOMED,DEPT BIOQUIM MED,POB 68041 BR-21941590 RIO JANEIRO BRAZIL ESCOLA TECN FED QUIM RIO DE JANEIRO BR-20010000 RIO JANEIRO BRAZIL UNIV ESTADUAL NORTE FLUMINENSE,CTR BIOCIENCIAS & BIOTECNOL,LAB QUIM &FUNCAO PROT & PEPTIDEOS BR-28015620 S JOSE CAMPOS RJ BRAZIL
Titolo Testata:
The Journal of biological chemistry
fascicolo: 47, volume: 271, anno: 1996,
pagine: 30227 - 30232
SICI:
0021-9258(1996)271:47<30227:IOACPF>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
YOLK PROTEINS; VITELLOGENIN GENE; ELECTROPHORETIC GELS; PHOSVITIN; LIPOVITELLIN; EMBRYOGENESIS; EVOLUTION; VITELLIN; SEQUENCE; PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
56
Recensione:
Indirizzi per estratti:
Citazione:
M.A.C. Silvaneto et al., "ISOLATION OF A CALCIUM-BINDING PHOSPHOPROTEIN FROM THE OOCYTES AND HEMOLYMPH OF THE BLOODSUCKING INSECT RHODNIUS-PROLIXUS", The Journal of biological chemistry, 271(47), 1996, pp. 30227-30232

Abstract

A novel calcium-binding phosphoprotein was isolated from the oocytes of the blood-sucking bug Rhodnius prolixus. This protein exhibits an apparent molecular mass of 18 kDa on gel filtration, but migrates as an8-kDa band on bis(hydroxymethyl)ethyl]glycine/SDS-polyacrylamide gels. It has a high content of serine (24% of the total number of residues), and phosphoserine is the sole amino acid phosphorylated in vivo. A similar protein was partially purified from the hemolymph. It resembles the oocyte form of the protein in its NH2-terminal sequence and its ability to be taken up by growing ovaries. Ca-45 binding to the oocytephosphoprotein was determined after SDS-polyacrylamide gel electrophoresis followed by blotting on nitrocellulose membranes. Titration of Ca2+-binding sites shows a high capacity (congruent to 50 mol/mol of protein), but a low affinity (K-0.5, congruent to 10(-3) M). Based on these characteristics, we have named this protein Rhodnius calcium-binding phosphoprotein, It resembles phosvitin, a phosphoprotein present inthe oocytes of nonmammalian vertebrates.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 21:15:55