The relationship between Candida species charge density and chitosan activity evaluated by ion-exchange chromatography

2011 ◽  
Vol 879 (31) ◽  
pp. 3749-3751 ◽  
Author(s):  
A. Palmeira-de-Oliveira ◽  
L.A. Passarinha ◽  
C. Gaspar ◽  
R. Palmeira-de-Oliveira ◽  
B. Sarmento ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Charge Density ◽  
Candida Species ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
The Relationship

scholarly journals Bovine liver thiol-protein disulphide oxidoreductases. An alternative method for differential purification and resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase

1980 ◽  
Vol 191 (2) ◽  
pp. 389-393 ◽  
Author(s):  
D A Hillson ◽  
R B Freedman
Keyword(s):  
Ion Exchange ◽  
Rapid Method ◽  
Bovine Liver ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Protein Disulphide Isomerase ◽  
The Relationship ◽  
Thiol Protein ◽  
Homogeneous Preparation ◽  
Covalent Chromatography

1. Protein disulphide-isomerase (EC 5.3.4.1) and glutathione-insulin transhydrogenase (EC 1.8.4.2) activities in bovine liver were studied in parallel during purification of ‘thiol-protein disulphide oxidoreductase’ by the procedure of Carmichael, Morin & Dixon [(1977) J Biol. Chem. 252, 7163-7167]. The two activities showed no quantitative co-purification and were partially resolved by (NH4)SO4 precipitation, indicating that distinct enzymes are present. 2. Protein disulphide-isomerase was purified by a relatively rapid method involving a combination of the early stages of the Carmichael procedure and covalent chromatography, with a new stepwise elution procedure. Ion-exchange chromatography yields a homogeneous preparation of mol.wt. 57 000. 3. The relationship between protein disulphide-isomerase, glutathione-insulin transhydrogenase and ‘thiol-protein disulphide oxidoreductase’ is discussed.

THE RELATIONSHIP OF RADIOIMMUNOASSAY TO BIOASSAY: IN VITRO STUDIES WITH SYNTHETIC LYSINE VASOPRESSIN IN AQUEOUS SOLUTION INACTIVATED BY HEAT

1978 ◽  
Vol 88 (3) ◽  
pp. 465-473 ◽  
Author(s):  
Hanne Løve Lembøl
Keyword(s):  
Aqueous Solution ◽  
Ion Exchange ◽  
Arginine Vasopressin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Lysine Vasopressin ◽  
Relationship Of ◽  
The Relationship ◽  
Immunological Heterogeneity

ABSTRACT The relationship of radioimmunoassay to pressor assay and antidiuretic assay was investigated in a simple in vitro system of synthetic lysine vasopressin in aqueous solution inactivated by heating at 100°C for 9, 18, 27, 36, 54 and 72 h. An apparent dissociation between radioimmunoassay and bioassay was demonstrated, with biological activity being lost more rapidly than immunological activity. The half-times were 32 h for radioimmunoassay, 23 h for antidiuretic assay and 22 h for pressor assay. However, ion-exchange chromatography showed immunological heterogeneity but biological homogeneity of the lysine vasopressin used, and indicated that the presence of impurities in the vasopressin might to some extent explain the discrepancy between assay results. Synthetic arginine vasopressin and arginine vasopressin of pituitary origin showed a similar immunological heterogeneity by ion-exchange chromatography.

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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