Isolation of Soluble HL-A Antigens from Normal Human Sera by Ion Exchange Chromatography

2008 ◽  
Vol 3 (5) ◽  
pp. 251-256 ◽  
Author(s):  
R. J. Billing ◽  
K. K. Mittal ◽  
P. I. Terasaki
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Human Sera ◽  
Normal Human

Isolation of 2-Acetamido-1-β-(L-β-Aspartamido)-1,2-Dideoxy-D-Glucose from Normal Human Urine

1972 ◽  
Vol 18 (9) ◽  
pp. 951-955 ◽  
Author(s):  
Barbara O’Neill Rowley ◽  
Paul B Hamilton
Keyword(s):  
Ion Exchange ◽  
Human Urine ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Normal Individuals ◽  
Normal Human ◽  
Elution Behavior ◽  
Solvent Systems ◽  
And Migration ◽  
Layer Chromatography

Abstract A glycopeptide was isolated from normal human urine by fractionation on a column of Sephadex G-10 and preparative ion-exchange chromatography. Elution behavior during ion-exchange chromatography in two different solvent systems, amino acids formed upon hydrolysis, and migration on high-voltage electrophoresis and thin-layer chromatography were essentially identical for this substance and for authentic 2-acetamido-l-β-(L-β-aspartamido)-1,2-dideoxy-D-glucose. A technique was developed to permit analytical-scale fractionation of individual urines followed by analysis for this glycopeptide; urine from two normal individuals contained 7 and 11 µmol of 2-acetamido-1-β-(L-β-aspartamido)-1,2-dideoxy-D-glucose per liter.

Studies on γA-globulins and α2-macroglobulins. Characterization of γA- and α2-macroglobulins

1968 ◽  
Vol 46 (3) ◽  
pp. 211-216 ◽  
Author(s):  
Benjamin E. Sanders ◽  
Yang H. Oh
Keyword(s):  
Ion Exchange ◽  
Physicochemical Properties ◽  
Human Plasma ◽  
Molecular Sieve ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Normal Human Plasma ◽  
Γ Globulins ◽  
Normal Human

Fractionation into several individual components was achieved from Cohn's Fraction III of human plasma by the successive application of separation principles that depend on solubility, charge, and size (precipitation, ion-exchange chromatography, and molecular-sieve chromatography methods). Characterization was made by various electrophoretic procedures such as microzone on cellulose acetate, disc on acrylamide gel, and immunoelectrophoresis, and includes some physicochemical properties of the purified proteins. There are found to be various components of γ-globulins, α2-macroglobulins, β-glycoproteins, β-lipoproteins, and other minor proteins in Cohn's Fraction III of normal human plasma. The physicochemical properties of two γA-globulins and two α2-macroglobulins were investigated.

STUDIES ON THE NATURE OF MAMMALIAN HYPOTHALAMIC THYROTROPHIN RELEASING HORMONE USING IMMUNOCHEMICAL, CHROMATOGRAPHIC AND ENZYMIC TECHNIQUES

1975 ◽  
Vol 65 (1) ◽  
pp. 83-90 ◽  
Author(s):  
S. L. JEFFCOATE ◽  
N. WHITE
Keyword(s):  
Ion Exchange ◽  
Human Plasma ◽  
Carboxymethyl Cellulose ◽  
Mammalian Species ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Normal Human Plasma ◽  
Thyrotrophin Releasing Hormone ◽  
Releasing Hormone ◽  
Normal Human

SUMMARY Hypothalamic extracts from three mammalian species (rat, rabbit and sheep) were found to contain several ng of immunoreactive thyrotrophin releasing hormone (TRH)-like activity. This substance chromatographed on ion exchange chromatography (carboxymethyl cellulose) as a single peak that was indistinguishable from synthetic TRH. Hypothalamic TRH was also inactivated by normal human plasma at a rate (1·21–1·46%/μl plasma/h and 1·59–1·77%/50 μl plasma/min) similar to that of synthetic TRH (1·42%/μl plasma/h and 1·73%/50 μl plasma/min). This combination of chromatographic and enzymic techniques can be applied to the identification of immunoreactive TRH in body fluids.

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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