Detection of fungal carbohydrate antigens by high-performance immunoafnity chromatography using a protein A column with covalently linked immunoglobulin G

Ruiter, G.A. de; Smid, P.; Schols, H.A.; Boom, Jacques H. van; Rombouts, F.M.

doi:10.1016/0378-4347(92)80010-n

Cited by 6 publications

(6 citation statements)

References 23 publications

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“…This lysate was cleared by centrifugation at 20 817 RCF for 2 × 20 min and the resulting supernatant incubated batchwise with Protein A Sepharose Cl‐4B (GE healthcare) coupled to either W6/32, recognizing an antigenic determinant common to HLA‐A, ‐B, ‐C, ‐E, ‐F and ‐G, or B27‐M1 antibodies (WEHI Antibody Facility, Australia), as per De Ruiter et al. (De Ruiter et al., ) as modified by Purcell et al. (Purcell, ; Purcell and Gorman, ) (10 mg/ml resin, as indicated).…”

Section: Methodsmentioning

confidence: 99%

Exploration of peptides bound to MHC class I molecules in melanoma

Pritchard

Hastie

Neller

et al. 2015

Pigment Cell Melanoma Res

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Advancements in high-resolution HPLC and mass spectrometry have reinvigorated the application of this technology to identify peptides eluted from immunopurified MHC class I molecules. Three melanoma cell lines were assessed using w6/32 isolation, peptide elution and HPLC purification; peptides were identified by mass spectrometry. A total of 13,829 peptides were identified; 83-87% of these were 8-11 mers. Only approximately 15% have been described before. Subcellular locations of the source proteins showed even sampling; mRNA expression and total protein length were predictive of the number of peptides detected from a single protein. HLA-type binding prediction for 10,078 9/10 mer peptides assigned 88-95% to a patient-specific HLA subtype, revealing a disparity in strength of predicted binding. HLA-B*27-specific isolation successfully identified some peptides not found using w6/32. Sixty peptides were selected for immune screening, based on source protein and predicted HLA binding; no new peptides recognized by antimelanoma T cells were discovered. Additionally, mass spectrometry was unable to identify several epitopes targeted ex vivo by one patient's T cells.

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Section: Methodsmentioning

confidence: 99%

Exploration of peptides bound to MHC class I molecules in melanoma

Pritchard

Hastie

Neller

et al. 2015

Pigment Cell Melanoma Res

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“…Immobilized proteins and microorganisms are used in bioreactors, , affinity chromatography, , immunoassays, , biosensors, , clinical analysis and diagnostics, − and environmental monitoring . One of the main concerns regarding the use of immobilized proteins is the loss of biological activity upon immobilization.…”

Section: Introductionmentioning

confidence: 99%

Cytochrome c Recognition of Immobilized, Orientational Variants of Cytochrome b₅: Direct Force and Equilibrium Binding Measurements

et al. 1999

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Direct force measurements, surface plasmon resonance spectroscopy, and genetic manipulations were used to investigate the impact of the orientation of immobilized cytochrome b5 (cyt b5) on its interactions with cytochrome c (cyt c). In this work, we used two cyt b5 orientational variants that present different regions of the protein surface when immobilized. Direct force measurements demonstrated that the two orientations generate a small difference in the electrostatic surface potential of the protein monolayers, in agreement with the calculated electrostatic potential distribution across the protein surface. This difference did not result in any differences in the electrostatic force between cyt c and the cyt b5 variants, however. The measured equilibrium binding constant for the cyt c interaction with cyt b5 also did not depend on the orientation of the latter. These results suggest that, at large separations, cyt c initially interacts relatively nonspecifically with a large patch of negative charge on the cyt b5. At short separations, it then adopts the optimum relative orientation for electron transfer. The force measurements not only elucidated the molecular basis of the equilibrium binding behavior, but also the possible molecular mechanisms that govern the interactions between these proteins in solution.

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“…Immobilization of protein film assemblies on solid substrates is of widespread interest because they are a key component in molecular devices such as biosensors (Swalen et al, 1987;Arnold and Meyerhoff, 1988) and affinitybased chromatographic supports (Hage and Kao, 1991;De Ruiter, 1992). In general, the ligand binding site(s) comprises a relatively small fraction of the total surface area of a protein.…”

Section: Introductionmentioning

confidence: 99%

Molecular Orientation Distributions in Protein Films: III. Yeast Cytochrome c Immobilized on Pyridyl Disulfide-Capped Phospholipid Bilayers

Edmiston

Saavedra

1998

Biophysical Journal

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Molecular orientation in a hydrated monolayer film of yeast cytochrome c, immobilized via disulfide bonding between Cys-102 and a pyridyl disulfide-capped phospholipid bilayer deposited from an air-water interface onto glass substrates, was investigated. The orientation distribution of the heme groups in the protein film was determined using a combination of absorption linear dichroism, measured in a planarintegrated optical waveguide-attenuated total reflection geometry- and fluorescence anisotropy, measured in a total internal reflection geometry. A gaussian model for the orientation distribution was used to recover the mean heme tilt angle and angular distribution about the mean, which were 40 and 11 degrees, respectively. Additional experiments showed that a large fraction of the cytochrome c was disulfide bonded to the bilayer, which correlates with the high degree of macroscopic order in the protein film. However, a subpopulation of yeast cytochrome c molecules in the film (approximately 30% of the total) appeared to be nonspecifically adsorbed. The orientation distribution of this subpopulation was found to be much broader than the specifically bound fraction.

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Detection of fungal carbohydrate antigens by high-performance immunoafnity chromatography using a protein A column with covalently linked immunoglobulin G

Cited by 6 publications

References 23 publications

Exploration of peptides bound to MHC class I molecules in melanoma

Exploration of peptides bound to MHC class I molecules in melanoma

Cytochrome c Recognition of Immobilized, Orientational Variants of Cytochrome b₅: Direct Force and Equilibrium Binding Measurements

Molecular Orientation Distributions in Protein Films: III. Yeast Cytochrome c Immobilized on Pyridyl Disulfide-Capped Phospholipid Bilayers

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Detection of fungal carbohydrate antigens by high-performance immunoafnity chromatography using a protein A column with covalently linked immunoglobulin G

Cited by 6 publications

References 23 publications

Exploration of peptides bound to MHC class I molecules in melanoma

Exploration of peptides bound to MHC class I molecules in melanoma

Cytochrome c Recognition of Immobilized, Orientational Variants of Cytochrome b5: Direct Force and Equilibrium Binding Measurements

Molecular Orientation Distributions in Protein Films: III. Yeast Cytochrome c Immobilized on Pyridyl Disulfide-Capped Phospholipid Bilayers

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Cytochrome c Recognition of Immobilized, Orientational Variants of Cytochrome b₅: Direct Force and Equilibrium Binding Measurements