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Titolo:
Proteins immunoreactive with antibody against a human leptin fragment are found in serum and tissues of the sea lamprey, Petromyzon marinus L
Autore:
Yaghoubian, S; Filosa, MF; Youson, JH;
Indirizzi:
Univ Toronto, Div Life Sci, Dept Zool, Scarborough, ON M1C 1A4, Canada Univ Toronto Scarborough ON Canada M1C 1A4 carborough, ON M1C 1A4, Canada
Titolo Testata:
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
fascicolo: 4, volume: 129, anno: 2001,
pagine: 777 - 785
SICI:
1096-4959(200107)129:4<777:PIWAAA>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
OBESE GENE; METAMORPHOSIS; EXPRESSION; TEMPERATURE; LARVAL; HORMONES; RECEPTOR; INSULIN; CLONING; MICE;
Keywords:
crossreactive proteins; fat metabolism; lamprey; leptin; leptin antibody; metamorphosis; Petromyzon marinus; serum proteins;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Filosa, MF Univ Toronto, Div Life Sci, Dept Zool, 1265 Mil Trail, Scarborough, ON M1C1A4, Canada Univ Toronto 1265 Mil Trail Scarborough ON Canada M1C 1A4 anada
Citazione:
S. Yaghoubian et al., "Proteins immunoreactive with antibody against a human leptin fragment are found in serum and tissues of the sea lamprey, Petromyzon marinus L", COMP BIOC B, 129(4), 2001, pp. 777-785

Abstract

An affinity-purified, polyclonal antibody raised against a peptide corresponding to amino acids 137-156 at the carboxy terminus of human leptin (16 kD) was used to search for immunoreactive protein(s) in the lamprey, Petromyzon marinus. Immunoblots of serum from different phases of the life cycle showed the presence of a 65-kD immunoreactive protein in the larvae and all stages of metamorphosis but not in feeding juvenile and upstream migrant adults. Extracts of tissues known to store fat were also examined using the same antibody. Muscle and fat column from all phases tested (larvae, stage 2and 4 metamorphosing animals, feeding juveniles and upstream migrants) showed 100- and 50-kD immunoreactive proteins. Extracts of nephric fold, the primary site of fat storage during metamorphosis, lacked the 100-kD protein but had the 50 kD; they also had a 16 kD immunoreactive protein not found in the other tissues. The immunoreactivity of the proteins of both serum andtissue extracts was blocked by pretreatment of the antibody with the leptin-derived antigen. The results indicate that P. marinus has proteins that share at least one epitope with mammalian leptin. (C) 2001 Elsevier Science Inc. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 07:39:34