Simulation of mono-PEGylated lysozyme separation in heparin affinity chromatography using a general rate model

2017 ◽  
Vol 93 (7) ◽  
pp. 1980-1987 ◽  
Author(s):  
Luis Alberto Mejía-Manzano ◽  
Gabriela Sandoval ◽  
M Elena Lienqueo ◽  
Pablo Moisset ◽  
Marco Rito-Palomares ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Rate Model ◽  
Heparin Affinity

A novel purification strategy for retrovirus gene therapy vectors using heparin affinity chromatography

2005 ◽  
Vol 90 (4) ◽  
pp. 391-404 ◽  
Author(s):  
Mar�a de las Mercedes Segura ◽  
Amine Kamen ◽  
Pierre Trudel ◽  
Alain Garnier
Keyword(s):  
Gene Therapy ◽  
Affinity Chromatography ◽  
Gene Therapy Vectors ◽  
Heparin Affinity

Purification of Retrovirus Particles Using Heparin Affinity Chromatography

2008 ◽  
pp. 1-11 ◽  
Author(s):  
María Mercedes Segura ◽  
Amine Kamen ◽  
Alain Garnier
Keyword(s):  
Affinity Chromatography ◽  
Heparin Affinity

scholarly journals Separation of virus-like particles and extracellular vesicles by flow-through and heparin affinity chromatography

2019 ◽  
Vol 1588 ◽  
pp. 77-84 ◽  
Author(s):  
Katrin Reiter ◽  
Patricia Pereira Aguilar ◽  
Viktoria Wetter ◽  
Petra Steppert ◽  
Andres Tover ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Extracellular Vesicles ◽  
Virus Like Particles ◽  
Flow Through ◽  
Heparin Affinity

Heparin-Affinity of Antithrombin III in a Family With Congenital Antithrombin III Deficiency

1979 ◽  
Author(s):  
G. Sas ◽  
D. Bánhegyi ◽  
I. Petö
Keyword(s):  
Affinity Chromatography ◽  
Antithrombin Iii ◽  
Normal Person ◽  
Agarose Gel ◽  
Functional Methods ◽  
At Iii ◽  
Antithrombin Iii Deficiency ◽  
Heparin Affinity

We found a new thrombophilic family with antithrombin III/ AT-III / deficiency. In the members of this family both immunologic and functional methods revealed similarly decreased levels of AT-III. Gelfiltration displayed identical size of AT-III molecule of patient and normal alike. On the basis of tnese findings we assumed that in this family normal AT-III is produced Dut only in diminished quantity. Experiments on the heparin-affinity of AT-III did not support this assumption. The AT-III of the proposita migrated slower than that of normal person in the heparinized agarose gel. In the course of the heparin-affinity chromatography the AT-III of the proposita could be eluted at lower salt concentrations than normal AT-III.Thus we conclude that even in the case of “true” AT-III deficiency the molecule might have some qualitative deviation from normal.

Optimized purification of mono-PEGylated lysozyme by heparin affinity chromatography using response surface methodology

2017 ◽  
Vol 92 (10) ◽  
pp. 2554-2562 ◽  
Author(s):  
Luis Alberto Mejía-Manzano ◽  
M Elena Lienqueo ◽  
Edgardo J Escalante-Vázquez ◽  
Marco Rito-Palomares ◽  
Juan A Asenjo
Keyword(s):  
Response Surface Methodology ◽  
Affinity Chromatography ◽  
Response Surface ◽  
Heparin Affinity

Separation of mouse crushed muscle extract into distinct mitogenic activities by heparin affinity chromatography

1994 ◽  
Vol 160 (3) ◽  
pp. 563-572 ◽  
Author(s):  
Gang Chen ◽  
Zipora Yablonka-Reuveni ◽  
Lebris S. Quinn ◽  
Roger S. Birnbaum
Keyword(s):  
Affinity Chromatography ◽  
Muscle Extract ◽  
Heparin Affinity

scholarly journals Amelioration of the severity of heparin-binding antithrombin mutations by posttranslational mosaicism

Blood ◽  
2012 ◽  
Vol 120 (4) ◽  
pp. 900-904 ◽  
Author(s):  
Irene Martínez-Martínez ◽  
José Navarro-Fernández ◽  
Alice Østergaard ◽  
Ricardo Gutiérrez-Gallego ◽  
José Padilla ◽  
...  
Keyword(s):  
Affinity Chromatography ◽  
Binding Domain ◽  
Heparin Binding ◽  
Wild Type ◽  
Antithrombin Deficiency ◽  
Thrombotic Risk ◽  
Heparin Binding Domain ◽  
New Type ◽  
Fluorescence Kinetic ◽  
Heparin Affinity

The balance between actions of procoagulant and anticoagulant factors protects organisms from bleeding and thrombosis. Thus, antithrombin deficiency increases the risk of thrombosis, and complete quantitative deficiency results in intrauterine lethality. However, patients homozygous for L99F or R47C antithrombin mutations are viable. These mutations do not modify the folding or secretion of the protein, but abolish the glycosaminoglycan-induced activation of antithrombin by affecting the heparin-binding domain. We speculated that the natural β-glycoform of antithrombin might compensate for the effect of heparin-binding mutations. We purified α- and β-antithrombin glycoforms from plasma of 2 homozygous L99F patients. Heparin affinity chromatography and intrinsic fluorescence kinetic analyses demonstrated that the reduced heparin affinity of the α-L99F glycoform (KD, 107.9 ± 3nM) was restored in the β-L99F glycoform (KD, 53.9 ± 5nM) to values close to the activity of α-wild type (KD, 43.9 ± 0.4nM). Accordingly, the β-L99F glycoform was fully activated by heparin. Similar results were observed for recombinant R47C and P41L, other heparin-binding antithrombin mutants. In conclusion, we identified a new type of mosaicism associated with mutations causing heparin-binding defects in antithrombin. The presence of a fully functional β-glycoform together with the activity retained by these variants helps to explain the viability of homozygous and the milder thrombotic risk of heterozygous patients with these specific antithrombin mutations.

Sign in / Sign up

Export Citation Format

Share Document