ISSN:
1572-8943
Keywords:
affinity chromatography
;
biopharmaceutics
;
conformational epitope
;
differential scanning calorimetry
;
ELISA
;
gp120
;
multidomain protein
;
OKT4a
;
protein stability
;
sCD4
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract Differential scanning calorimetry (DSC) was used, in conjunction with two functional assays that monitor binding, in a storage stability study on a protein of pharmaceutical interest, the soluble form of the T-lymphocyte multidomain surface receptor, sCD4. DSC monitored structural changes in binding and non-binding domains. ELISA, using the monoclonal antibody OKT4a, and frontal elution affinity chromatography, using the HIV surface glycoprotein, gp120, monitored function of the binding domain. The stability of sCD4 in a solution formulation was followed for up to 30 days at five differentpHs ranging from 5.0 to 7.9 and five different temperatures ranging from −70
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01992848
Permalink