The influence of salt type on the retention of bovine serum albumin in ion-exchange chromatography

2007 ◽  
Vol 1139 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Sattar Al-Jibbouri
Keyword(s):  
Bovine Serum Albumin ◽  
Ion Exchange ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography

scholarly journals REAGINIC ACTIVITY ASSOCIATED WITH IGG IMMUNOGLOBULIN

1966 ◽  
Vol 123 (5) ◽  
pp. 845-858 ◽  
Author(s):  
Robert T. Reid ◽  
Percy Minden ◽  
Richard S. Farr
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Anion Exchange ◽  
Bovine Serum ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Unique Property ◽  
Serum Fractions ◽  
Human Sera

Five human sera with reaginic activity to a number of allergens were fractionated using anion exchange chromatography. In each serum, fractions which contained detectable IgG and no detectable IgA had capacity to fix to skin and subsequently elicit a P-K reaction. Four of these sera had reaginic activity about equally distributed between fractions containing only IgG and fractions containing mixtures of IgG and IgA. A fifth serum contained reaginic activity to crystalline bovine serum albumin (BSA) and most of the activity was associated with the fraction which contained only IgG. This serum was extensively studied using a variety of techniques and it was confirmed that most of the reagin to BSA in this serum was in those fractions containing only IgG. Since reaginic activity can no longer be considered a unique property of IgA the implications of finding antibody with reaginic qualities in immunoglobulins other than IgA are discussed.

Ion-exchange equilibria of lysozyme myoglobin and bovine serum albumin

1989 ◽  
Vol 465 (3) ◽  
pp. 137-156 ◽  
Author(s):  
R.D. Whitley ◽  
R. Wachter ◽  
F. Liu ◽  
N.-H.L. Wang
Keyword(s):  
Bovine Serum Albumin ◽  
Ion Exchange ◽  
Serum Albumin ◽  
Bovine Serum

Effects of the isolation methodology on protein profiles of blood trypomastigotes of Trypanosoma cruzi

Parasitology ◽  
2003 ◽  
Vol 126 (1) ◽  
pp. 41-51 ◽  
Author(s):  
C. HÖLSCHER ◽  
R. HARTMANN ◽  
H. MOSSMANN ◽  
G. A. SCHAUB
Keyword(s):  
Molecular Weight ◽  
Bovine Serum Albumin ◽  
Trypanosoma Cruzi ◽  
Serum Albumin ◽  
High Molecular Weight ◽  
Centrifugal Force ◽  
Bovine Serum ◽  
Exchange Chromatography ◽  
Protein Supplementation ◽  
Surface Proteins

Blood trypomastigotes of Trypanosoma cruzi were isolated from infected athymic rnu/rnu rats and purified by an improved procedure of DEAE-Sephacel ion-exchange chromatography. Elution into a buffer supplemented with bovine serum albumin avoided column-induced changes on the surface of the parasites. Biotin-labelled bovine serum albumin, fluorescence microscopy, flow cytometry and Western blot analysis revealed a very intense binding of albumin to the parasite. Incubation and washing of cells without protein supplementation did not result in any damage or lysis of parasites but it did cause extensive shedding of cellular and surface proteins into the supernatant which could be prevented by using the protein-supplemented buffer. A decreasing yield of high molecular weight cellular proteins in relation to centrifugal force was a general phenomenon observed in scanning densitometry of SDS gels after isolation in either protein-supplemented buffer or protein-free buffer. The quantity of shed cellular components increased with increasing centrifugal force. In contrast, quantities of high molecular weight, biotin-labelled surface proteins increased with greater centrifugal force, indicating labelling of otherwise inaccessible residues. These data emphasize the importance of protein supplementation of buffers with proteins and of choosing low centrifugation forces (<400 g) during investigations of T. cruzi.

Purification and Properties of an Antiactivator Fraction from Bovine Serum

1979 ◽  
Vol 42 (03) ◽  
pp. 855-863 ◽  
Author(s):  
L B Nanninga ◽  
M M Guest
Keyword(s):  
Molecular Weight ◽  
Ion Exchange ◽  
Dissociation Constant ◽  
Bovine Serum ◽  
Gamma Globulin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Low Concentrations ◽  
Purification And Properties ◽  
Free Serum

SummaryA method is described for the purification of antiactivator from bovine euglobulin-free serum by means of gelfiltration and ion exchange chromatography. The purified antiactivator has no antifibrinolytic activity. It has a molecular weight of about 115,000 and it appears to be a gamma globulin. The dissociation constant of its complex with urokinase is 1.6 X 10-9 M and the maximum urokinase binding is close to 2000 CTA units per mg. Its concentration in bovine serum is 0.37%. Flufenamate displaces urokinase from the antiactivator at very low concentrations, about 10-4 M. Cysteine restores its activity if lost by standing. Also an antifibrinolysin fraction is obtained free of antiactivator activity.

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