Data di Pubblicazione:
1983
Citazione:
Interaction of alpha 2-HS-glycoprotein with immobilized triazine dyes / P. Arnaud, D.L. Emerson, E. Gianazza. - In: BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY. - ISSN 0167-4838. - 749:3(1983), pp. 270-275. [10.1016/0167-4838(83)90235-2]
Abstract:
We studied the interaction of α2-HS-glycoprotein with immobilized Cibacron blue F3-GA (Blue A) and Procion red HE-3B (Red A). When whole plasma was applied on the Blue A, α2-HS-glycoprotein remained unbound, together with other plasma proteins. In contrast, when this fraction was applied on the Red A, α2-HS-glycoprotein was shown to bind tightly and was eluted with a linear sodium chloride gradient between 0.5 and 0.8 M. This proved to be a useful two-step technique for the purification of α2-HS-glycoprotein. Further characterization revealed that the protein appeared homogeneous by immunoelectrophoresis and SDS-polyacrylamide gel electrophoresis with yields greater than 30%. A small (< 5%) but significant fraction of α2-HS-glycorprotein with a same molecular weight as the native protein was consistently found in the wash of the Red A column, and may correspond to α2-HS-glycoprotein bound to a yet unidentified ligand.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
(Human serum); Affinity chromatography; Immobilized dye; α-2-HS-glycoprotein (human) purification
Elenco autori:
P. Arnaud, D.L. Emerson, E. Gianazza
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