Separation and purification of rice oryzenin subunits by anion-exchange and gel-permeation chromatography

1992 ◽  
Vol 40 (9) ◽  
pp. 1599-1601 ◽  
Author(s):  
Zigrida. Zarins ◽  
Joseph. Chrastil
Keyword(s):  
Anion Exchange ◽  
Gel Permeation Chromatography ◽  
Separation And Purification ◽  
Gel Permeation

Analysis of 188Re-EDTMP complexes by HPLC and ultrafiltration

2004 ◽  
Vol 92 (4-6) ◽  
Author(s):  
Kazuyuki Hashimoto ◽  
Hiromitsu Matsuoka
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Anion Exchange ◽  
High Performance ◽  
Gel Permeation Chromatography ◽  
Reversed Phase ◽  
Ion Pair ◽  
Gel Permeation

AbstractHigh performance liquid chromatography (anion-exchange, reversed-phase ion-pair and gel permeation chromatography) and ultrafiltration have been employed to analyze

SHORT COMMUNICATIONS Preparative-scale fractionation of bovine, caprine and ovine whey proteins by gel permeation chromatography

1997 ◽  
Vol 64 (3) ◽  
pp. 459-464 ◽  
Author(s):  
XAVIER FELIPE ◽  
ANDREW J. R. LAW
Keyword(s):  
Whey Protein ◽  
Anion Exchange ◽  
Whey Proteins ◽  
Gel Permeation Chromatography ◽  
Reversed Phase ◽  
Complete Separation ◽  
Protein Fractions ◽  
Rapid Preparation ◽  
Preparative Scale ◽  
Gel Permeation

The whey proteins of the cow, goat and sheep have previously been fractionated on an analytical scale by reversed-phase HPLC (De Frutos et al. 1992), anion-exchange FPLC (Andrews et al. 1985; Manji et al. 1985; Laezza et al. 1991) and gel permeation FPLC (Andrews et al. 1985; Hill & Kakuda, 1990). Anion-exchange and gel permeation FPLC can readily be scaled up for laboratory preparation of whey protein fractions. There is some indication, however, that anion-exchange FPLC does not give complete separation of β-lactoglobulin and α-lactalbumin from the other minor whey protein fractions (Girardet et al. 1989).In previous work it has been shown that gel permeation FPLC gives a satisfactory fractionation of the whey proteins of the cow (Law et al. 1993), goat (Law & Brown, 1994) and sheep (Law, 1995). In this paper we describe a scaled-up method of gel permeation that can be used for fairly rapid preparation or purification of four main whey protein fractions from the milks of these species.

scholarly journals Skeletal keratan sulphate chains isolated from bovine intervertebral disc may terminate in α(2----6)-linked N-acetylneuraminic acid

1992 ◽  
Vol 282 (1) ◽  
pp. 267-271 ◽  
Author(s):  
J M Dickenson ◽  
T N Huckerby ◽  
I A Nieduszynski
Keyword(s):  
Intervertebral Disc ◽  
Anion Exchange ◽  
Gel Permeation Chromatography ◽  
Intervertebral Discs ◽  
Borohydride Reduction ◽  
Anion Exchange Column ◽  
Keratan Sulphate ◽  
Acetylneuraminic Acid ◽  
Sialidase Inhibitor ◽  
Gel Permeation

Peptido-keratan sulphate fragments were isolated from the nucleus pulposus of bovine intervertebral discs (2-year-old animals) after digestion with chondroitin ABC lyase followed by digestion with diphenylcarbamoyl chloride-treated trypsin of A1D1 proteoglycans and gel-permeation chromatography on Sepharose CL-6B. The peptido-keratan sulphate fragments were subjected to alkaline borohydride reduction. The reduced chains were treated with keratanase in the presence of the sialidase inhibitor 2,3-dehydro-2-deoxy-N-acetylneuraminic acid, and the digest was subjected to alkaline borohydride reduction. This produced oligosaccharides with galactitol at their reducing ends. This reduced digest was chromatographed on a Nucleosil 5 SB anion-exchange column and individual oligosaccharides were isolated. One of these was shown by 600 MHz 1H-n.m.r. spectroscopy to have the following structure: NeuAc alpha 2-6Gal beta 1-4GlcNAc(6-SO4)beta 1-3Gal-ol The structure of this oligosaccharide shows that keratan sulphate chains from bovine intervertebral disc have non-reducing termini with N-acetylneuraminic acid linked alpha(2----6) as well as alpha(2----3) to an unsulphated galactose.

Aggregated, Conformationally Changed Fibrinogen Exposes the Stimulating Sites for t-PA-Catalysed Plasminogen Activation

1996 ◽  
Vol 75 (02) ◽  
pp. 326-331 ◽  
Author(s):  
Unni Haddeland ◽  
Knut Sletten ◽  
Anne Bennick ◽  
Willem Nieuwenhuizen ◽  
Frank Brosstad
Keyword(s):  
Conformational Changes ◽  
Gel Permeation Chromatography ◽  
Tissue Type ◽  
Plasminogen Activation ◽  
Chromogenic Substrate ◽  
Type Plasminogen Activator ◽  
Gel Permeation ◽  
Self Association ◽  
Fibrin Monomers ◽  
Stimulation Of

SummaryThe present paper shows that conformationally changed fibrinogen can expose the sites Aα-(148-160) and γ-(312-324) involved in stimulation of the tissue-type plasminogen activator (t-PA)-catalysed plasminogen activation. The exposure of the stimulating sites was determined by ELISA using mABs directed to these sites, and was shown to coincide with stimulation of t-PA-catalysed plasminogen activation as assessed in an assay using a chromogenic substrate for plasmin. Gel permeation chromatography of fibrinogen conformationally changed by heat (46.5° C for 25 min) demonstrated the presence of both aggregated and monomeric fibrinogen. The aggregated fibrinogen, but not the monomeric fibrinogen, had exposed the epitopes Aα-(148-160) and γ-(312-324) involved in t-PA-stimulation. Fibrinogen subjected to heat in the presence of 3 mM of the tetrapeptide GPRP neither aggregates nor exposes the rate-enhancing sites. Thus, aggregation and exposure of t-PA-stimulating sites in fibrinogen seem to be related phenomena, and it is tempting to believe that the exposure of stimulating sites is a consequence of the conformational changes that occur during aggregation, or self-association. Fibrin monomers kept in a monomeric state by a final GPRP concentration of 3 mM do not expose the epitopes Aα-(148-160) and γ-(312-324) involved in t-PA-stimulation, whereas dilution of GPRP to a concentration that is no longer anti-polymerizing, results in exposure of these sites. Consequently, the exposure of t-PA-stimulating sites in fibrin as well is due to the conformational changes that occur during selfassociation.

Gel Permeation Chromatography of Polyelectrolytes

1981 ◽  
Vol 4 (8) ◽  
pp. 1297-1309 ◽  
Author(s):  
M. Rinaudo ◽  
J. Desbrières ◽  
C. Rochas
Keyword(s):  
Gel Permeation Chromatography ◽  
Gel Permeation
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