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Titolo:
Is the unique negatively charged polypeptide of crayfish yolk HDL a component of crustacean vitellin?
Autore:
Abdu, U; Yehezkel, G; Weil, S; Ziv, T; Sagi, A;
Indirizzi:
Ben Gurion Univ Negev, Dept Life Sci, IL-84105 Beer Sheva, Israel Ben Gurion Univ Negev Beer Sheva Israel IL-84105 4105 Beer Sheva, Israel Technion Israel Inst Technol, Fac Biol, Prot Res Ctr, Haifa, Israel Technion Israel Inst Technol Haifa Israel , Prot Res Ctr, Haifa, Israel
Titolo Testata:
JOURNAL OF EXPERIMENTAL ZOOLOGY
fascicolo: 3, volume: 290, anno: 2001,
pagine: 218 - 226
SICI:
0022-104X(20010801)290:3<218:ITUNCP>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
MATURE FEMALE HEMOLYMPH; CHERAX-QUADRICARINATUS; PROTEIN VITELLOGENIN; CALLINECTES-SAPIDUS; OVARIAN MATURATION; PENAEUS-CHINENSIS; BLUE-CRAB; PRAWN; PURIFICATION; DEGRADATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
25
Recensione:
Indirizzi per estratti:
Indirizzo: Sagi, A Ben Gurion Univ Negev, Dept Life Sci, POB 653, IL-84105 Beer Sheva, Israel Ben Gurion Univ Negev POB 653 Beer Sheva Israel IL-84105 , Israel
Citazione:
U. Abdu et al., "Is the unique negatively charged polypeptide of crayfish yolk HDL a component of crustacean vitellin?", J EXP ZOOL, 290(3), 2001, pp. 218-226

Abstract

The yolk protein of Cherax quadricarinatus contains six major high-densitylipoprotein (HDL) subunits with the approximate molecular masses of 177, 155, 106, 95, 86, and 75 kDa, of which only the 106-kDa polypeptide is negatively charged. On the basis of their molecular weights, time of appearance and disappearance, their floating density and susceptibility to enzyme degradation (by a serine proteinase), these six HDL polypeptides were classified into two subgroups. One group comprises the higher-molecular-weight compounds above 106 kDa, and the other includes the lower-molecular-weight compounds up to 95 kDa. Other than being different from the lower-molecular-weight polypeptides, the negatively charged 106-kDa polypeptide was significantly different from members of its higher-molecular-weight group belonging toa different, less abundant, yolk protein as shown by HPLC separation. Immunological studies and peptide mapping in which the 106-kDa polypeptide did not show similarity to any of the other HDL components confirmed these differences. Moreover, the amino acid composition of the 106-kDa polypeptide was different from that of known vitellin from other crustacean species. Thisunique negatively charged polypeptide presents an enigma as it is known tobe a secondary vitellogenic-related HDL polypeptide, immunolocalized in yolk globules; however, it is different to all the other HDL polypeptides, thus presenting the question whether it is indeed a component of "classical" crustacean vitellin. (C) 2001 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 04:30:47