scholarly journals Preparation of nanogel-immobilized porous gel beads for affinity separation of proteins: fusion of nano and micro gel materials

2014 ◽  
Vol 47 (2) ◽  
pp. 220-225 ◽  
Author(s):  
Yu Hoshino ◽  
Yuka Arata ◽  
Yusuke Yonamine ◽  
Shih-Hui Lee ◽  
Aki Yamasaki ◽  
...  
1990 ◽  
pp. 335-344 ◽  
Author(s):  
T. Franco ◽  
B. A. Andrews ◽  
O. Cascone ◽  
C. Hodgson ◽  
A. T. Andrews ◽  
...  

1988 ◽  
Vol 175 (1) ◽  
pp. 154-161 ◽  
Author(s):  
Per-Åke Albertsson ◽  
Gerd Birkenmeier

2014 ◽  
Vol 34 ◽  
pp. 468-473 ◽  
Author(s):  
Xueyan Zou ◽  
Kun Li ◽  
Yanbin Yin ◽  
Yanbao Zhao ◽  
Yu Zhang ◽  
...  

2003 ◽  
Vol 24 (4) ◽  
pp. 577-581 ◽  
Author(s):  
Marina Cretich ◽  
Giovanna Pirri ◽  
Giacomo Carrea ◽  
Marcella Chiari

2018 ◽  
Vol 13 (1) ◽  
Author(s):  
Xueyan Zou ◽  
Fengbo Yang ◽  
Xin Sun ◽  
Mingming Qin ◽  
Yanbao Zhao ◽  
...  

2008 ◽  
Vol 9 (3) ◽  
pp. 828-833 ◽  
Author(s):  
Yusuke Goto ◽  
Ryosuke Matsuno ◽  
Tomohiro Konno ◽  
Madoka Takai ◽  
Kazuhiko Ishihara

1998 ◽  
Vol 799 (1-2) ◽  
pp. 83-91 ◽  
Author(s):  
M.Yakup Arıca ◽  
H.Nur Testereci ◽  
Adil Denizli

1978 ◽  
Vol 39 (01) ◽  
pp. 193-200 ◽  
Author(s):  
Erwin F Workman ◽  
Roger L Lundblad

SummaryAn improved method for the preparation of bovine α-thrombin is described. The procedure involves the activation of partially purified prothrombin with tissue thromboplastin followed by chromatography on Sulfopropyl-Sephadex C-50. The purified enzyme is homogeneous on polyacrylamide discontinuous gel electrophoresis and has a specific activity toward fibrinogen of 2,200–2,700 N.I.H. U/mg. Its stability on storage in liquid media is dependent on both ionic strenght and temperature. Increasing ionic strength and decreasing temperature result in optimal stability. The denaturation of α-thrombin by guanidine hydrochloride was found to be a partially reversible process with the renatured species possessing properties similar to “aged” thrombin. In addition, the catalytic properties of a-thrombin covalently attached to agarose gel beads were also examined. The activity of the immobilized enzyme toward fibrinogen was affected to a much greater extent than was the hydrolysis of low molecular weight, synthetic substrates.


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