A simple method of detection and isolation of oligosaccharides, fragments of chitosan after ion-exchange chromatography

1969 ◽  
Vol 18 (11) ◽  
pp. 2417-2419 ◽  
Author(s):  
V. I. Maksimov ◽  
V. A. Mosin
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Simple Method

A Simple Method to Screen for Radiostrontium in Water by Ion Exchange Chromatography

2019 ◽  
Vol 116 (6) ◽  
pp. 771-775
Author(s):  
Dao M. Nguyen ◽  
W. Allen Moody ◽  
John A. Williamson
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Simple Method

scholarly journals A rapid and simple method for the purification of transglutaminase from Streptoverticillium mobaraense.

1994 ◽  
Vol 299 (3) ◽  
pp. 825-829 ◽  
Author(s):  
U Gerber ◽  
U Jucknischke ◽  
S Putzien ◽  
H L Fuchsbauer
Keyword(s):  
Ion Exchange ◽  
Storage Stability ◽  
Culture Fluid ◽  
Strong Acid ◽  
Weak Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Single Step ◽  
Simple Method ◽  
High Yields

Transglutaminase from Streptoverticillium mobaraense was partially purified by ion-exchange chromatography on a weak acid material and hydrophobic chromatography. The separation with a strong acid ion-exchanger produces homogeneous transglutaminase, in a single step and with high yields, directly from the centrifuged and filtered culture fluid of the micro-organism. The procedure reproduced several times could be also carried out on a larger scale with the optimized parameters of the laboratory isolations. The purified enzyme demonstrated good storage stability.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

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