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Biomedical subjects

C Schafer-Nielsen

Publications and source records attributed to C Schafer-Nielsen.

8 recordsLinked to original sources
PubMed2002

Surface immunoglobulin on B lymphocytes as a potential target for specific peptide ligands in chronic lymphocytic leukaemia.

With the aim of producing unique targets for malignant cells we have identified peptide ligands for the clonal surface immunoglobulin isolated from the B cells of a chronic lymphocytic leukaemia (CLL) patient. The peptides were identified from random-peptide phage-display libraries. The obtained ligands bound specifically to the surface of the target lymphocytes as well as to clonal immunoglobulin in lysate from the same cells. Peptide-based antigen mimotopes may have a future use in targeted therapy of CLL and other B-cell-derived malignancies displaying surface immunoglobulin.

Amino Acid Sequence↗
PubMed1999

Identification of patient-specific peptides for detection of M-proteins and myeloma cells.

We have taken advantage of the selection power of phage display technology to define specific peptide mimotopes that recognize individual M-proteins, isolated from patients with multiple myeloma. Preferred amino acid motifs of phages binding to M-proteins were identified in 6/9 patients investigated. Chemically synthesized peptides, corresponding to the phage-displayed peptide inserts, were used to verify the specificity of binding in competition assays. The peptides were able to bind to the M-proteins, as well as the myeloma cells, with high sensitivity and specificity. Employing simple immunological techniques, < 0.01 g/l of M-protein could be quantified, suggesting a novel way for monitoring minimal residual disease in the production of guidelines for adjusting or reintroducing conventional chemotherapy. The peptide mimotopes defined by this technology may be useful as tumour-specific targeting agents and as a tool for purging cells in autologous bone marrow transplantation.

Adult↗
PubMed1995

A computer model for time-based simulation of electrophoresis systems with freely defined initial and boundary conditions.

A PC-based program has been developed that allows the user to perform one-dimensional computer simulations of electrophoresis systems with freely definable initial- and boundary conditions. The program can handle n constituents with n pK-values and calculates constituent concentrations and derived parameters as a function of time. Results are displayed graphically on screen and are stored as data files for graphical hard-copy processing.

Computer Simulation↗
PubMed1993

A flow-through microsampling device applied to an ion-exchange chromatography system.

A flow-through microsampling device that can be inserted in the column elution flow line of a chromatographic system has been developed. A sample drop (volume 2.2 nl) is ejected when a voltage pulse is applied to a piezo-electric transducer. The drops can be ejected with up to 70 Hz frequency, giving a sample flow range of 0-9 microliters/min. Samples were collected on a moving agarose surface during elution of freshly prepared human serum. The precipitate pattern obtained after immunoelectrophoresis is similar to what would be obtained in a fused rocket electrophoresis of multiple samples from a fraction collector.

Blood Proteins↗
PubMed1986

Divinylsulphone-activated agarose. Formation of stable and non-leaking affinity matrices by immobilization of immunoglobulins and other proteins.

Divinylsulphone-activated agarose is an attractive alternative to several of the activated supports usually used. Unlike CNBr-activated gels, it does not leak the immobilized protein at high pH. It reacts readily with proteins at near-neutral pH (unlike the epoxy-activated supports). Generally, divinylsulphone-activated agarose reacts with amino, hydroxyl, and sulphydryl groups, thus allowing immobilization of a wide spectrum of ligands. Moreover, it is available in an aqueous suspension free of organic solvents and neither requires time-consuming swelling nor washing.

Animals↗
PubMed1982

Separation of nucleic acids and chromatin proteins by hydrophobic interaction chromatography.

A procedure by which chromatin proteins (histones and non-histones) can be rapidly separated from nucleic acids by hydrophobic interaction chromatography is described. The procedure is carried out under non-rigorous conditions that must be assumed to induce little irreversible change in the biological properties of most proteins. More than 90% (w/w) of the chromatin proteins can be retained by hydrophobic interaction while nucleic acids pass quantitatively through the columns. By gradient elution of the columns the histones can be divided into fractions containing H1, H2A/H2B and H3/H4, and at the same time a subfractionation of the non-histone proteins is obtained. Protein recovery depends on the type of column used, but exceeds 80% (w/w) with even the most strongly binding hydrophobic matrix investigated.

Animals↗
PubMed1980

Separation of macromolecules in isotachophoresis systems involving single or multiple counterions.

The isotachophoresis principle provides unique opportunities for rational designs of fractionation procedures involving molecules. Theoretically any two charged molecules that are soluble under the experimental conditions involved can be physically separated if their electrophoretic net mobilities differ only slightly in the electrophoresis medium used. A theoretical and practical outline is presented that enables the reader to set up this fractionation system and on a rational basis develop fractionationprocedures for a given set of charged macromolecules by isotachophoresis with simple and well characterized ampholytes as spacer substances. The planning of preparative experiments in this approach is based on results obtained from rapid analytical screens on a microgram scale. The report includes an appendix containing the theoretical basis for computation of buffer compositions in the isotachophoretic steady state with mono/polyvalent constituents in systems involving one or more counterions and controlled amounts of interfering ions.

Blood Proteins↗