Literature DB >> 12504180

One step purification of alpha(1)-acid glycoprotein from human plasma. Fractionation of its polymorphic allele products.

Federica Azzimonti1, Daniel H Atchley, Catherine Anne Morrison, Seetal Dodd, David W Boulton, C Lindsay DeVane, Philippe Arnaud.   

Abstract

Alpha(1)-acid glycoprotein is a plasma protein that exhibits both microheterogeneity and polymorphism. Its purification from human plasma is usually performed using a sequence of different fractionation steps. Here we report a one-step isolation technique of this protein based upon pseudo-ligand affinity chromatography on immobilized Cibacron Blue F3GA at acidic pH. In addition, the use of two narrow pH elution buffers allows us to separate the two genetic products of this protein, which differ from each other by 21 amino acid substitutions. This technique will facilitate the study of the structural, biological and pharmacokinetic properties of each individual allele product.

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Year:  2003        PMID: 12504180     DOI: 10.1016/s1570-0232(02)00749-3

Source DB:  PubMed          Journal:  J Chromatogr B Analyt Technol Biomed Life Sci        ISSN: 1570-0232            Impact factor:   3.205


  2 in total

1.  Comparison of methods for the purification of alpha-1 acid glycoprotein from human plasma.

Authors:  Teresa R McCurdy; Varsha Bhakta; Louise J Eltringham-Smith; Sharon Gataiance; Alison E Fox-Robichaud; William P Sheffield
Journal:  J Biomed Biotechnol       Date:  2011-03-08

2.  The Carbohydrate-linked Phosphorylcholine of the Parasitic Nematode Product ES-62 Modulates Complement Activation.

Authors:  Umul Kulthum Ahmed; N Claire Maller; Asif J Iqbal; Lamyaa Al-Riyami; William Harnett; John G Raynes
Journal:  J Biol Chem       Date:  2016-04-04       Impact factor: 5.157

  2 in total

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