Purification and partial characterization of an arginine binding molecule from human placenta

A binding molecule for L-arginine has been isolated from human placental membranes and partially characterized. It exhibits specificity for L-arginine almost exclusively with no apparent cooperativity of binding as seen by Scatchard analysis (K d = 0.36nM). Enzymatic probes indicate a molecule conta...

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Veröffentlicht in:	Life sciences (1973) 1982-06, Vol.30 (23), p.1973-1979
Hauptverfasser:	Cornwell, Trudy, Collins, Steven, Aglio, Linda S., Maturo, Joseph M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Arginine - metabolism Carrier Proteins - isolation & purification Carrier Proteins - metabolism Chemical Phenomena Chemistry Chymotrypsin - pharmacology Female Galactosidases - pharmacology Glycoside Hydrolases - pharmacology Humans Placenta - analysis Pregnancy Substrate Specificity Trypsin - pharmacology Type C Phospholipases - pharmacology
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Beschreibung
Zusammenfassung:	A binding molecule for L-arginine has been isolated from human placental membranes and partially characterized. It exhibits specificity for L-arginine almost exclusively with no apparent cooperativity of binding as seen by Scatchard analysis (K d = 0.36nM). Enzymatic probes indicate a molecule containing important carbohydrate and lipid moieties.
ISSN:	0024-3205 1879-0631
DOI:	10.1016/0024-3205(82)90436-2