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Titolo:
CHARACTERIZATION OF VITELLOGENIN AND VITELLIN FROM LAND CRAB POTAMON POTAMIOS - IDENTIFICATION OF A PRECURSOR POLYPEPTIDE IN THE MOLECULE
Autore:
PATERAKI LE; STRATAKIS E;
Indirizzi:
UNIV CRETE,DEPT BIOL,POB 1470 IRAKLION 71110 CRETE GREECE UNIV CRETE,DEPT BIOL IRAKLION 71110 CRETE GREECE
Titolo Testata:
The Journal of experimental zoology
fascicolo: 6, volume: 279, anno: 1997,
pagine: 597 - 608
SICI:
0022-104X(1997)279:6<597:COVAVF>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
HIGH-DENSITY LIPOPROTEINS; MATURE FEMALE HEMOLYMPH; FRESH-WATER PRAWN; PENAEUS-MONODON; MACROBRACHIUM-ROSENBERGII; MALACOSTRACAN CRUSTACEA; PROTEIN VITELLOGENIN; UCA-PUGILATOR; FIDDLER CRAB; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
52
Recensione:
Indirizzi per estratti:
Citazione:
L.E. Pateraki e E. Stratakis, "CHARACTERIZATION OF VITELLOGENIN AND VITELLIN FROM LAND CRAB POTAMON POTAMIOS - IDENTIFICATION OF A PRECURSOR POLYPEPTIDE IN THE MOLECULE", The Journal of experimental zoology, 279(6), 1997, pp. 597-608

Abstract

A female-specific protein, vitellogenin (Vg), and its corresponding egg vitellin (Vn) were identified in the land crab Potamon potamios. Electrophoretic analysis of the hemolymph protein during the annual reproduction cycle revealed that the processing of vitellogenesis did not occur in males or in females of a previtellogenic stage. The analysis of ovarian and egg extracts revealed the presence of Vn, which was identical to Vg. Both Vg and Vn were present in three different aggregational states that represented monomeric, dimeric, and trimeric species of the proteins. In both proteins, the predominant form was the dimeric, which had a molecular mass of 551 kDa for Vg and 510 kDa for Vn. Under denaturing conditions, each of the individual Vg and Vn aggregatesreleased three polypeptides with molecular masses of 115, 105, and 85kDa. In spite of the difference in terms of native molecular mass, the Vg and Vn were similar in their lipid, carotenoid, and carbohydrate composition. However, Vg of some animals contained a fourth polypeptide with a molecular mass of 181 kDa. This polypeptide and the three other Vg and Vn polypeptides were immunoreactive against anti-Vg preparedfrom the 85 kDa Vg polypeptide. Furthermore, proteolytic cleavage experiments confirmed that the 115 and 105 kDa Vg polypeptides were derived from the 181 kDa polypeptide. We conclude that the presence of the 181 kDa polypeptide in the Vg molecule resulted in the higher molecular mass of Vg. (C) 1997 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 05:07:07