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PubMed1989

Binding of ions and hydrophobic probes to alpha-lactalbumin and kappa-casein as determined by analytical affinity chromatography.

The technique of analytical affinity chromatography was extended to characterize binding of ions and hydrophobic probes to proteins. Using the immobilized protein mode of chromatography, alpha-lactalbumin and kappa-casein were covalently attached to 200-nm-pore-diameter controlled-pore glass beads and accommodated for high-performance liquid chromatography. The existence of a high affinity binding site (Kdiss = 0.16 microM) (site I) for calcium ion in alpha-lactalbumin was confirmed by chromatography of [45Ca2+]. In addition, chromatography of the hydrophobic probes, 1-(phenylamino)-8-naphthalene-sulfonate (ANS)2 and 4,4'-bis[1-(phenylamino)-8-naphthalenesulfonate (bis-ANS) indicated that Ca2+ bound to a second site (presumably the zinc site or site II) with weaker affinity. Dissociation constants obtained for apo-alpha-lactalbumin were about 80 microM for ANS and 4.7 microM for bis-ANS in the absence of sodium ion. Addition of Ca2+ initially caused a reduction in surface hydrophobicity (lowered affinity for the probe dyes) followed by an increase at higher Ca2+ concentrations (greater than 0.5 mM), suggesting that occupancy of site II restores an apo-like conformation to the protein. Moreover, the effect of Zn2+ was similar to that observed in the higher Ca2+ concentration range, whereas Na+ apparently bound to site I. A calcium binding site of moderate affinity also exists in kappa-casein (Kdiss = 15.6 microM). A cluster of negative charges, probably including the orthophosphate group, most likely comprise this binding site. By preventing self-association, analytical affinity chromatography permits microscale characterization of ligand equilibria in proteins that are unaffected by protein-protein interactions.

Animals↗
PubMed1988

Chromatography of serum on Sep-pak C18 corrects falsely elevated vitamin D metabolite levels measured by protein binding assay.

Using a commercial kit method we obtained a vitamin D metabolite level within the normal range in a patient with biopsy-proven osteomalacia. This suggested that the ethanol extraction method employed had not removed serum factors known to falsely elevate the measurement of vitamin D metabolites. We therefore compared the levels measured after ethanol extraction and after purification by chromatography on Sep-pak C18 or Sephadex LH-20. Vitamin D metabolite levels after ethanol extraction of sera correlated with, but were higher than, those after chromatography on Sep-pak C18 cartridges (r = 0.84; 134 +/- 76 vs 76 +/- 46 nmol/l: mean +/- SD; p less than 0.01). Results were similar after chromatography on Sep-pak C18 and Sephadex LH-20 (r = 0.95; 79 +/- 46 vs 68 +/- 41 nmol/l). Sera from 5 patients (4 with osteomalacia, 1 with chronic pancreatitis/malabsorption) had vitamin D metabolite levels in the normal range after ethanol extraction but had low levels after Sep-pak C18 chromatography; four of these sera also had low levels after chromatography on Sephadex LH-20. These findings indicate that chromatography of serum on Sep-pak C18 cartridges corrects falsely elevated vitamin D metabolite levels measured by protein binding assay.

Adult↗
PubMed2005

Anion chromatography using on-line recycled eluents.

Non-suppressed anion chromatography, using on-line recycled eluents, was investigated. Cations and anions from samples were excluded from the eluents using a mixture of strongly acidic cation-exchange resins and strongly basic anion exchange resins in the eluent reservoir. This exclusion was performed after determination of the anions in the non-suppressed anion chromatography, and the eluents were then recycled on-line. The performance of consecutive determinations was evaluated from the relative standard deviation (RSD) of peak heights and retention times of chloride, bromide, nitrite, nitrate, and sulfate ions, with a concentration of 3 microg ml(-1) each, compared to that of normal anion chromatography. Over 50 consecutive determinations could be achieved with an eluent volume of only 200 ml for a 100 microl sample volume. Almost all the RSD values for retention time, and peak heights of these anions, were smaller than 3%. Over fifty consecutive determinations of chloride, nitrate, and sulfate ions in a river water sample could be achieved with an eluent volume of only 100 ml. All the RSD values for retention time and peak heights of these anions were smaller than 3%. The eluent volume could be decreased to one tenth of that used in normal anion chromatography. The performance of the anion chromatography, using on-line recycled eluents, was the same as that for normal anion chromatography under the same conditions.

Anions↗
PubMed2006

Large-scale recovery of C-phycocyanin from Spirulina platensis using expanded bed adsorption chromatography.

C-phycocyanin was purified on a large scale by a combination of expanded bed adsorption, anion-exchange chromatography and hydroxyapatite chromatography from inferior Spirulina platensis that cannot be used for human consumption. First, phycobiliproteins were extracted by a simple, scaleable method and then were recovered by Phenyl-Sepharose chromatography in an expanded bed column. The purity (the A(620)/A(280) ratio) of C-phycocyanin isolated with STREAMLINE column was up to 2.87, and the yield was as high as 31 mg/g of dried S. platensis. After the first step, we used conventional anion-exchange chromatography for the purification steps, with a yield of 7.7 mg/g of dried S. platensis at a purity greater than 3.2 and with an A(620)/A(650) index higher than 5.0. The fractions from anion-exchange chromatography with a level of purity that did not conform to the above standard were subjected to hydroxyapatite chromatography, with a C-PC yield of 4.45 mg/g of dried S. platensis with a purity greater than 3.2. The protein from both purification methods showed one absolute absorption peak at 620 nm and a fluorescence maximum at 650 nm, which is consistent with the typical spectrum of C-phycocyanin. SDS-PAGE gave two bands corresponding to 21 and 18 kDa. In-gel digestion and LC-ESI-MS showed that the protein is C-phycocyanin.

Adsorption↗
PubMed1981

Purification and studies of components of the haemostatic system by affinity chromatography.

The application of affinity chromatographic techniques for separations and studies on molecular interactions of the components of the blood coagulation system is reviewed. Most of the components have been purified using processes involving one or several affinity chromatographic steps. Many different kinds of affinity chromatography have been used, including inhibitor interaction chromatography, effector interaction chromatography, immunosorption, hydrophobic interaction chromatography, metal chelate chromatography and covalent chromatography. Affinity chromatographic techniques have also been used to study molecular interactions such as the fibrin polymerization process. One example of large-scale purification of a clinically used component is given.

Blood Chemical Analysis↗
PubMed1990

High-performance displacement chromatography-mass spectrometry of tryptic peptides of recombinant human growth hormone.

The combination of high-performance displacement chromatography with continuous flow fast atom bombardment (FAB)-mass spectrometry (MS) offers a means of overcoming the sample capacity limitations imposed by the low flow-rates tolerated in microbore systems employed for directly coupled liquid chromatography-MS. Displacement chromatography is performed at high concentrations with the same equipment and columns as typically used in chromatography at low concentrations. By using this mode of chromatography with a solution of cetyltrimethylammonium bromide as the displacer, the capacity of a reversed-phase column can be increased 50- to 100-fold for separation of a tryptic digest of biosynthetic human growth hormone. Despite the high load, the use of displacement chromatography allowed high-resolution separation of the complex mixture of eighteen major components. On-line analysis by continuous flow FAB-MS yielded high-quality spectra of these peptides and demonstrated that sharp, single-component bands can be obtained in this separation. Along with the major fragments, the chromatogram showed other peptides originating from protein variants in the sample, from non-specific cleavage in the enzymatic digest or from autolysis of trypsin. On-line analysis also allowed selective ion monitoring of the column effluent for individual peptides and confirmed the high efficiency and resolution obtained by preparative displacement separations on HPLC columns and equipment.

Amino Acid Sequence↗
PubMed1975

Silica gel thin-layer chromatography of acidic phospholipids. II. Chromatographic behaviour of phosphatidylserine and phosphatidic acid applied with different cation composition on adsorbents either free of metal ions or containing a surplus of divalent metal ions.

Different salt forms of phosphatidylserine and phosphatidic acid (two acidic phospholipids) have been subjected to thin-layer chromatography on two commonly used silica adsorbents, one of which (silica gel HR) is practically free of metal ions and the other (silica gel G) contains 13% of calcium sulphate as binder. The chromatographic behaviour was studied in an acidic, a neutral and a basic solvent. Both adsorbents provided usable systems for phosphatidylserine with each of the three solvents, except for silica gel G with the neutral solvent, in which system tailing was prominent. The inclusion of calcium sulphate in the silica gel tended to impair chromatography of phosphatidylserine in acidic and neutral solvents, but improved its chromatography in the basic solvent. In all the systems, the migration was independent of the cation composition of the applied phosphatidylserine samples. For the chromatography of phosphatidic acid, only three of the systems tested were usable, and in those three, the chromatographic behaviour was independent of the cation composition of the samples. The calcium sulphate in an adsorbent increased tailing of phosphatidic acid in acidic and neutral solvents, as it did for phosphatidylserine, whereas with the basic solvent, calcium sulphate in the adsorbent caused phosphatidic acid to remain at the origin. Two one-dimensional thin-layer chromatographic systems previously recommended for the chromatography of acidic phospholipids were unsuitable for the chromatography of phosphatidic acid under the conditions used here. For both phosphatidylserine and phosphatidic acid chromatographed in acidic systems, the solvent must contain water in addition to acetic acid if excessive tailing is to be avoided.

Calcium↗
PubMed1989

High-performance liquid chromatography of amino acids, peptides and proteins. XCIII. Comparison of methods for the purification of mouse monoclonal immunoglobulin M autoantibodies.

A comparison of methods for the purification of naturally occurring mouse monoclonal autoantibodies, of the immunoglobulin M (IgM) isotype, has been performed to determine the optimal strategies for the isolation of IgM from ascites fluid and in vitro tissue culture hybridoma supernatants. In order to quantify each purification procedure, the concentration of IgM in eluted fractions was determined by using a double-sandwich mu-chain-specific anti-IgM enzyme-linked immunosorbent assay, and the purity of the IgM was determined by a bicinchoninic acid-based protein assay and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The most efficient single-step purification was based on size-exclusion chromatography on high-resolution Superose 6 HR 10/30 fast protein liquid chromatography (FPLC) columns. This procedure resulted in recoveries of monoclonal IgMs of ca. 71-86% with purities between 68 and 86%. Single-step chromatography of monoclonal IgM, on Superose 6 FPLC columns resulted in a 21-fold purification of IgM, prepared by the in vitro culture of hybridoma cells in dialysis membrane. Size-exclusion chromatography, performed with Sephacryl S-300 columns, resulted in reduced resolution of monoclonal IgM, with yields of ca. 57-80% and purity of ca. 42-58% compared with the high-resolution Superose 6 FPLC columns. "Non-ideal" size-exclusion chromatography on Superose 6 FPLC columns resulted in selective retention of monoclonal IgMs and elution of IgM with high-ionic-strength buffers in the trailing peak. Recovery of IgM with this strategy was high (ca. 82-92%) but the purity was not comparable to the single-step fractionation of IgM on Superose 6 FPLC columns. Single-step anion- and cation-exchange and mixed-mode hydroxyapatite chromatography resulted in only partial purification of monoclonal IgM with the applied procedures. With these latter separation techniques, monoclonal IgM was eluted with a variety of other ascites fluid or supernatant proteins, including those with apparent molecular weights identical to those of mouse IgG and albumin. Sequential purification of monoclonal IgMs by Mono Q anion exchange, followed by Superose 6 FPLC columns, resulted in a 2- to 3-fold purification of IgM but did not separate IgM from high-molecular-weight contaminants with apparent molecular weights similar to those of alpha 2-macroglobulin and IgG. Enrichment of monoclonal IgM from ascites fluid by ammonium sulphate precipitation revealed increasing IgM recovery with increasing ammonium sulphate final concentrations up to 60%.(ABSTRACT TRUNCATED AT 400 WORDS)

Amino Acids↗
PubMed2002

Vacancy ion-exclusion chromatography of carboxylic acids on a weakly acidic cation-exchange resin.

In this preliminary study, a new approach to ion-exclusion chromatography is proposed to overcome the relatively poor conductivity detection response which occurs in ion-exclusion chromatography when acids are added to the eluent in order to improve peak shape. This approach, termed vacancy ion-exclusion chromatography, requires the sample to be used as eluent and a sample of water to be injected onto a weakly acidic cation-exchange column (TSKgel OApak-A). Vacancy peaks for each of the analytes appear at the retention times of these analytes. Highly sensitive conductivity detection is possible and sharp, well-shaped peaks are produced, leading to efficient separations. Retention times were found to be affected by the concentration of the analytes in the eluent, and also by the presence of an organic modifier such as methanol in the eluent. Detection limits for oxalic, formic, acetic, propionic, butyric and valeric acids were 0.1, 0.2, 0.3, 0.3, 0.4 and 0.5 microM, respectively, and linear ranges for some acids extended over two orders of magnitude. Precision values for retention times were 0.21% and for peak areas were <1.90%. The vacancy ion-exclusion chromatography method was found to give detection responses four to 10 times higher than conventional ion-exclusion chromatography using sulfuric acid eluent and two to five times higher than conventional ion-exclusion chromatography using benzoic acid eluent.

Cation Exchange Resins↗
PubMed2002

Miniaturized membrane-based reversed-phase chromatography and enzyme reactor for protein digestion, peptide separation, and protein identification using electrospray ionization mass spectrometry.

A commonly used capillary fitting is employed for housing miniaturized membrane chromatography for performing reversed-phase peptide separations. By placing a hydrophobic and porous polyvinylidene fluoride membrane around the end of a polymer sleeve, the assembly of capillary fitting not only provides the stationary phase, but also establishes the necessary flow paths using capillary connections. The miniaturized membrane chromatography system is coupled with a micro-enzyme reactor containing immobilized trypsins for performing rapid protein digestion, peptide separation, and protein identification using electrospray ionization mass spectrometry. Separation performance of cytochrome c digest in miniaturized membrane chromatography is compared with the results obtained from micro-LC and capillary LC. The efficacy and the potentials of miniaturized membrane chromatography in tryptic mapping are reported. The use of miniaturized membrane chromatography allows significant reduction in sample consumption together with enhanced detection sensitivity. By minimizing the void volume in miniaturized membrane chromatography, the elution times of cytochrome c peptides are significantly shortened in this study in comparison with our previous results, and are comparable with those in micro-LC and capillary LC using considerably higher mobile phase flow-rates.

Animals↗
PubMed2002

Purification of turkey coronavirus by Sephacryl size-exclusion chromatography.

Sephacryl S-1000 size-exclusion chromatography was used to purify turkey coronavirus (TCoV) from infected turkey embryo. TCoV was propagated in the 22-day-old turkey embryos. Intestines and intestinal contents of infected embryos were harvested and homogenized. After low speed centrifugation, the supernatant was concentrated by ultracentrifugation through a cushion of 30 or 60% sucrose solution, or by ammonium sulfate precipitation. The purification methods included sucrose gradient and Sephacryl S-1000 size-exclusion chromatography. Ultracentrifugation through a cushion of 60% sucrose solution was better than the other two methods for concentration of TCoV from intestinal homogenate. The most effective method for purifying TCoV and removing extraneous materials was size-exclusion chromatography as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. More spike-rich particles were observed in the sample purified by chromatography than those purified by sucrose gradient as examined by electron microscopy. Differentiation of turkey anti-TCoV antiserum from normal turkey serum was better achieved by ELISA plates coated with TCoV preparation purified by size-exclusion chromatography than that purified by sucrose density gradient. The results indicated that Sephacryl S-1000 chromatography was useful for purification of TCoV.

Animals↗
PubMed1984

Development and validation of a method for measuring the glycine and taurine conjugates of bile acids in bile by high-performance liquid chromatography.

We developed and validated a simple method for measuring the individual glycine and taurine conjugates of bile acids in bile by high-performance liquid chromatography with a C18 reversed-phase column using an isocratic solvent system of acidified methanol--potassium phosphate. Without preliminary derivatization or purification, complete separation of the ten major conjugated bile acids present in bile could be achieved in 65 min. Total bile acid concentrations were identical when measured enzymatically and by summing the individual bile acids determined by high-performance liquid chromatography. Bile acid composition determined by gas-liquid chromatography correlated with results by high-performance liquid chromatography. Finally, measurements of individual glycine and taurine conjugates in human bile and in mixtures of bile acid standards by high-performance liquid chromatography and thin-layer chromatography gave similar results. This high-performance liquid chromatographic system permits simultaneous quantification of total and individual bile acids and their glycine and taurine conjugates in bile.

Bile↗
PubMed1999

Comparison of different transition metal ions for immobilized metal affinity chromatography of selenoprotein P from human plasma.

Cu2+, Ni2+, Zn2+, Co2+ and Cd2+ were evaluated in metal ion affinity chromatography for enrichment of selenoprotein P, and immobilized Co2+ affinity chromatography was found to be the most selective chromatographic method. The chromatography was performed by fast protein liquid chromatography and the fractionation was followed by analysis of the collected fractions for selenium by inductively coupled plasma mass spectrometry. By the combination of immobilized Co2+ affinity chromatography and heparin affinity chromatography a simple method was developed yielding a 14,800-fold enrichment of selenoprotein P. The purity of the protein was determined by SDS-PAGE and by sequencing from polyvinylidene difluoride blots of SDS-PAGE gels.

Affinity Labels↗
PubMed1988

Purification of human pancreatic gamma-glutamyltranspeptidase by lectin affinity chromatography.

Two types of pancreatic gamma-glutamyltranspeptidase (GGTP) (EC 2.3.2.2), sialic acid poor and sialic acid rich, were purified by the following: anion-exchange chromatography, wheat germ agglutinin (WGA)-Sepharose chromatography, gel filtration chromatography, phenyl-Superose chromatography, and hydroxylapatite chromatography. Among these, WGA-Sepharose chromatography helped to increase the specific activity of the GGTPs by approximately 20-30-fold in one effort. On dodecyl sulfate polyacrylamide gel electrophoresis, the two pancreatic GGTPs had different molecular weights. Sialic acid-rich GGTP had two subunits of Mr 67,000 and 27,000; however, the sialic acid-poor type had two subunits of Mr 72,000 and 29,000. The pI value of the sialic acid-poor GGTP was 5.9, and that of the sialic acid-rich GGTP 3.6.

Chromatography, Affinity↗
PubMed1986

Establishment of beta-hydroxy fatty acids as chemical marker molecules for bacterial endotoxin by gas chromatography-mass spectrometry.

Selected ion-monitoring gas chromatography-mass spectrometry was used for detection of beta-hydroxy fatty acids as an independent assay for the presence or absence of endotoxin in materials claimed to induce nonspecific activation of Limulus amoebocyte lysate. To this end, suspensions of gram-negative and -positive bacteria, one fungal species, cerebrospinal fluid, and hollow-fiber hemodialyzer rinses were assayed for endotoxin by gas chromatography-mass spectrometry and the Limulus amoebocyte lysate assay. Good qualitative agreement was shown for both methods when suspensions of test organisms were assayed. Two false-negative results were obtained by gas chromatography-mass spectrometry assays of cerebrospinal fluid and were shown to be a result of insufficient endotoxin in the cerebrospinal fluid specimens for detection by gas chromatography-mass spectrometry. Hemodialyzer rinses were Limulus assay positive; however, no beta-hydroxy fatty acids were detected by gas chromatography-mass spectrometry. These data were compared with data obtained from USP rabbit pyrogen tests of the rinse materials (nonpyrogenic) and chemical characterization of the Limulus assay-reactive rinses, which showed the rinses to be cellulosic in nature. It is suggested that beta-hydroxy fatty acids, as assayed by selected ion-monitoring gas chromatography-mass spectrometry, be used as chemical marker molecules for the presence or absence of endotoxin in materials reported to cause nonspecific activation of Limulus amoebocyte lysate.

Candida albicans↗
PubMed2003

Strategy for analysis of cardiac troponins in biological samples with a combination of affinity chromatography and mass spectrometry.

BACKGROUND: Cardiac troponins are modified during ischemic injury and are found as a heterogeneous mixture in blood of patients with cardiovascular diseases. We present a strategy to isolate cardiac troponins from human biological material, by use of affinity chromatography, and to provide samples ready for direct analysis by mass spectrometry. METHODS: Cardiac troponins were isolated from human left ventricular tissue by affinity chromatography. Isolated troponins were either eluted and analyzed by Western blot or enzymatically digested while bound to affinity beads. The resulting peptide mixture was subjected to mass spectrometry for protein identification and characterization. The same method was used to analyze serum from patients with acute myocardial infarction (AMI). RESULTS: Affinity chromatography with antibodies specific for one cardiac troponin subunit facilitated the isolation of the entire cardiac troponin complex from myocardial tissue. The three different proteases used for enzymatic digestion increased the total protein amino acid sequence coverage by mass spectrometry for the three cardiac troponin subunits. Combined amino acid sequence coverage for cardiac troponin I, T, and C (cTnI, cTnT, cTnC) was 54%, 48%, and 40%, respectively. To simulate matrix effects on the affinity chromatography-mass spectrometry approach, we diluted tissue homogenate in cardiac troponin-free serum. Sequence coverage in this case was 44%, 41%, and 19%, respectively. Finally, affinity chromatography-mass spectrometry analysis of AMI serum revealed the presence of cardiac troponins in a wide variety of its free and/or complexed subunits, including the binary cTnI-cTnC and cTnI-cTnC-cTnT complexes. CONCLUSIONS: Affinity chromatography-mass spectrometry allows the extraction and analysis of cardiac troponins from biological samples in their natural forms. We were, for the first time, able to directly confirm the presence of cardiac troponin complexes in human serum after AMI. This approach could assist in more personalized risk stratification as well as the search for reference materials for cardiac troponin diagnostics.

Amino Acid Sequence↗
PubMedDate not supplied

Vancomycin monitoring in term newborns: comparison of peak and trough serum concentrations determined by high performance liquid chromatography and fluorescence polarization immunoassay.

INTRODUCTION: Peak and trough serum concentrations of vancomycin were determined in term newborn infants with confirmed or suspected Staphylococcus sp sepsis by high performance liquid chromatography and flourescence polarization immunoassay. OBJECTIVE: To statistically compare the results of the high performance liquid chromatography and flourescence polarization immunoassay techniques for measuring serum vancomycin concentrations. METHODS: Eighteen peak and 20 trough serum samples were assayed for vancomycin concentrations using high performance liquid chromatography and flourescence polarization immunoassay from October 1995 to October 1997. RESULTS: The linear correlation coefficients for high performance liquid chromatography and flourescence polarization immunoassay were 0.27 (peak, P = 0.110) and 0.26 (trough, P = 0.1045) respectively, which were not statistically significant. CONCLUSION: There was wide variation in serum vancomycin concentrations determined by high performance liquid chromatography as compared with those determined by flourescence polarization immunoassay. There was no recognizable pattern in the variability; in an apparently random fashion, the high performance liquid chromatography measurement was sometimes substantially higher than the flourescence polarization immunoassay measurement, and at other times it was substantially lower.

Anti-Bacterial Agents↗
PubMed2006

Ion-exchange chromatography used to isolate a spermadhesin-related protein from domestic goat (Capra hircus) seminal plasma.

Mammalian seminal plasma contains among others, proteins called spermadhesins, which are the major proteins of boar and stallion seminal plasma. These proteins appear to be involved in capacitation and sperm-egg interaction. Previously, we reported the presence of a protein related to spermadhesins in goat seminal plasma. In the present study, we have further characterized this protein, and we propose ion-exchange chromatography to isolate this seminal protein. Semen was obtained from four adult Saanen bucks. Seminal plasma was pooled, dialyzed against distilled water and freeze-dried. Lyophilized proteins were loaded onto an ion-exchange chromatography column. Dialyzed-lyophilized proteins from the main peak of DEAE-Sephacel were applied to a C2/C18 column coupled to an RP-HPLC system, and the eluted proteins were lyophilized for electrophoresis. The N-terminal was sequenced and amino acid sequence similarity was determined using CLUSTAL W. Additionally, proteins from DEAE-Sephacel chromatography step were dialyzed and submitted to a heparin-Sepharose high-performance liquid chromatography. Goat seminal plasma after ion-exchange chromatography yielded 6.47 +/- 0.63 mg (mean +/- SEM) of the major retained fraction. The protein was designated BSFP (buck seminal fluid protein). BSFP exhibited N-terminal sequence homology to boar, stallion and bull spermadhesins. BSFP showed no heparin-binding capabilities. These results together with our previous data indicate that goat seminal plasma contains a protein that is structurally related to proteins of the spermadhesin family. Finally, this protein can be efficiently isolated by ion-exchange and reverse-phase chromatography.

Animals↗