Literature DB >> 7067402

Interactions of different albumins and animal sera with insolubilized Cibacron Blue, Evaluation of apparent affinity constants.

J Naval, M Calvo, F Lampreave, A Piñeiro.   

Abstract

1. A high concentration Cibacron Blue-Sepharose derivative has been used to study the affinity chromatography of albumin from eight animal species. 2. The apparent affinity constants for albumin varies between 3.9 x 10(4) M-1 and 0.9 x 10(4) M-1, in the order: Human greater than rabbit greater than horse greater than pig = dog greater than bovine greater than rat greater than chicken. 3. Other serum proteins were also bound to the gel, particularly lipoproteins and alpha 2-macroglobulin.

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Year:  1982        PMID: 7067402     DOI: 10.1016/0305-0491(82)90401-1

Source DB:  PubMed          Journal:  Comp Biochem Physiol B        ISSN: 0305-0491


  2 in total

1.  Comparative studies of the binding of some ligands to human serum albumin non-covalently attached to immobilized Cibacron Blue, or covalently immobilized on Sepharose, by column affinity chromatography.

Authors:  C Lagercrantz; T Larsson
Journal:  Biochem J       Date:  1983-08-01       Impact factor: 3.857

2.  Trypanothione S-transferase activity in a trypanosomatid ribosomal elongation factor 1B.

Authors:  Tim J Vickers; Alan H Fairlamb
Journal:  J Biol Chem       Date:  2004-04-08       Impact factor: 5.157

  2 in total

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