Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Characterization of a folate receptor in parotid gland and folate binding protein in saliva from humans - Epitope relatedness to human milk folate binding protein
Autore:
Holm, J; Hansen, SI; Hoier-Madsen, M; Nichols, CW;
Indirizzi:
Herning Hosp, Dept Clin Chem, DK-7400 Herning, Denmark Herning Hosp Herning Denmark DK-7400 Clin Chem, DK-7400 Herning, Denmark Hillerod Hosp, Dept Clin Chem, Hillerod, Denmark Hillerod Hosp Hillerod Denmark Hosp, Dept Clin Chem, Hillerod, Denmark State Serum Inst, Lab Autoimmune Serol, Copenhagen, Denmark State Serum Inst Copenhagen Denmark toimmune Serol, Copenhagen, Denmark Genet & Lab Med, Atlanta, GA USA Genet & Lab Med Atlanta GA USAGenet & Lab Med, Atlanta, GA USA
Titolo Testata:
APMIS
fascicolo: 7-8, volume: 108, anno: 2000,
pagine: 517 - 524
SICI:
0903-4641(200007/08)108:7-8<517:COAFRI>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMINO-ACID-SEQUENCE; COWS MILK; KB CELLS; MEMBRANE; AFFINITY; LIGAND; SPECIFICITY; KIDNEY;
Keywords:
folate receptor; human salivary glands; salivary folate binding protein; epitope-relatedness to human milk folate binding protein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
32
Recensione:
Indirizzi per estratti:
Indirizzo: Holm, J Herning Hosp, Dept Clin Chem, DK-7400 Herning, Denmark Herning Hosp Herning Denmark DK-7400 m, DK-7400 Herning, Denmark
Citazione:
J. Holm et al., "Characterization of a folate receptor in parotid gland and folate binding protein in saliva from humans - Epitope relatedness to human milk folate binding protein", APMIS, 108(7-8), 2000, pp. 517-524

Abstract

The present study was performed to establish the antigenic identity and origin of the folate binding protein in human saliva. We identified a folate receptor in human parotid and submandibular gland which immunoreacted with antibodies against human milk folate binding protein, as evidenced by ELISAand immunostaining of ductal epithelium and secretory glandular material. The receptor concentration was 0.4-1.4 nmol H-3-folate bound/g protein. Ligand binding was of a high-affinity (K = 10(10) M-1) type, exhibited positive cooperativity, a slow radioligand dissociation at pH 7.4, and inhibition by folate analogues. The concentration of immunoreactive folate binding protein in saliva as determined by ELISA with antibodies against human milk folate binding protein was several fold higher than that determined by radioligand binding (nil - 1 nM). This indicates that a major fraction of the immunoreactive material does not bind H-3-folate, and could represent a precursor form of the protein. In conclusion, the folate binding protein in humansaliva seems to be a secretory product of the salivary glands. The proteinis also epitope-related to folate binding proteins in other human mucosal secretions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/11/20 alle ore 11:41:50