Immunoreactivity of Goat's Milk Casein Fractionated by Ion-Exchange Chromatography

1995 ◽  
Vol 43 (8) ◽  
pp. 2025-2029 ◽  
Author(s):  
Ana I. Haza ◽  
Paloma Morales ◽  
Rosario Martin ◽  
Teresa Garcia ◽  
Gonzalo Anguita ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Goat’S Milk ◽  
Goat's Milk ◽  
Milk Casein

Comparative study of the separation of casein from bovine, ovine and caprine milks using HPLC

1993 ◽  
Vol 60 (4) ◽  
pp. 495-504 ◽  
Author(s):  
Stelios E. Kaminarides ◽  
Emmanuel M. Anifantakis
Keyword(s):  
Ion Exchange ◽  
Comparative Study ◽  
Anion Exchange ◽  
Deae Cellulose ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Strong Anion Exchange ◽  
Milk Casein ◽  
Better Than

SummaryThe separation of cows', sheep's and goats' milk casein components by HPLC on a strong anion-exchange (P.L-SAX 8μ 1000A) column is described. During HLPC, whole caseins of the three kinds of milk behaved differently from conventional separations. The casein components of the three kinds of milk were well resolved under the Chromatographie conditions used. HPLC resolved the κ-caseins better than did ion-exchange chromatography on DEAE cellulose, and was particularly efficient in the case of goats' milk. Goats' and sheep's milks had almost similar Chromatographie profiles but these differed considerably from that of cows' milk. Caseins from the sheep and the goat were also similar in that a shallower NaCl gradient was required for the separation of casein components than for cows' milk.

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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