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Biomedical subjects

H Delincée

Publications and source records attributed to H Delincée.

7 recordsLinked to original sources
PubMed1975

Fractionation of horseradish peroxidase by preparative isoelectric focusing, gel chromatography and ion-exchange chromatography.

Horseradish peroxidase has been fractionated by preparative isoelectric focusing in a density gradient and in a layer of granulated gel using pH-3-10 and narrow-pH-range carrier ampholytes at different total enzyme loads. The resolution of peroxidase isoenzymes in preparative-layer isoelectric focusing was comparable to that obtained by analytical thin-layer isoelectric focusing. Isoelectrically homogeneous isoenzymes could be isolated with good recovery in a single fractionation step. Despite the excellent separation of the individual isoenzymes by isoelectric focusing in gel layers, an effective purification, indicated by the absorbance ratio A403mn/A278nm, could not be achieved by focusing applied as a single step. By different fractionation sequences combining gel chromatography, ion-exchange chromatography, and isoelectric focusing, individual isoenzymes with a high purity and homogeneous with respect to their size and charge properties have been isolated.

Chromatography, Gel↗
PubMed1975

Structural damage of gamma-irradiated ribonuclease revealed by thin-layer isoelectric focusing.

Ribonuclease, irradiated with 60Co gamma-rays in dilute aqueous solution or in the dry state, has been investigated with respect to its charge and size properties. Thin-layer isoelectric focusing revealed extensive change in irradiated RNase; new enzymatically-active components, mainly with isoelectric points lower than in unirradiated RNase were observed. Thin-layer gel chromatography indicated the formation of aggregates which are partially active enzymatically. Aggreation depended on enzyme concentration and was less in more dilute solutions-- at equal degrees of inactivation. Structural damage in the so-called 'native' monomers was revealed by thin-layer isoelectric focusing, their charge properties being distinctly modified.

Cobalt Radioisotopes↗
PubMedDate not supplied

[Radiation-induced aggregation of proteins: binding of amino acids to myoglobin (author's transl)].

When myoglobin is irradiated in the presence of amino acids, the most radiation-reactive species, like the aromatic and sulfur-containing amino acids, will bind preferentially to the protein. The radiation-induced binding is strongly dependent on the concentration of protein and amino acid. Subsequent to irradiation of myoglobin in the presence of radioactively labelled tryptophan followed by tryptic hydrolysis, only a single radioactive spot was detected on the fingerprint. The binding of amino acids is thus not randomly distributed over the protein molecule but occurs at specific reactive sites.

Amino Acids↗