BETA-D-GLUCANASES OF SCHIZOPHYLLUM COMMUNE

1967 ◽  
Vol 13 (8) ◽  
pp. 969-978
Author(s):  
G. L. Schneberger ◽  
W. W. Luchsinger
Keyword(s):  
Ion Exchange ◽  
Schizophyllum Commune ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Heat Inactivation ◽  
Inactivation Kinetics ◽  
Hydrolysis Products ◽  
Culture Filtrates

Culture filtrates of Schizophyllum commune have been subjected to ion-exchange chromatography, and the laminarin-splitting and endo-β-glucanase activities have been studied with respect to pH behavior, heat inactivation kinetics, effects of inhibitors, and hydrolysis products. Evidence is presented to show that the two activities may be due to the same enzyme and that a β-(1 → 3) linkage may be involved in the specificity of the enzyme.

Isolation and Fast Purification o f Neocarzinostatin by FPLC-Ion Exchange Chromatography

1983 ◽  
Vol 38 (11-12) ◽  
pp. 939-942
Keyword(s):  
Ion Exchange ◽  
Anion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
New Method ◽  
Clinical Grade ◽  
Anion Exchange Column ◽  
Exchange Column ◽  
Culture Filtrates ◽  
Reproducible Method

Neocarzinostatin, a highly toxic antitum or protein containing an essential nonprotein chromophore, can be isolated and purified from culture filtrates of Streptomyces carzinostaticus. Usually a lengthy procedure of up to 60 h is necessary for the isolation, including several chromatographic steps partly under conditions which favour inactivation of the drug by release of chromophore. We describe a new method yielding practically clinical grade Neocarzinostatin from crude extracts in 20 min. This very fast and reproducible method was made possible by using a Mono Q anion exchange column filled with monodisperse gel material which has been recently developed

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.

Review on the Application of Mixed-mode Chromatography for Separation of Structure Isoforms

2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa
Keyword(s):  
Ion Exchange ◽  
Mixed Mode ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Charged State ◽  
Partial Structure ◽  
Reverse Phase ◽  
Oligomer Formation ◽  
Structure Rearrangement ◽  
Disulfide Scrambling

Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.

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