Biomedical subjects

M Karel

Publications and source records attributed to M Karel.

At least 37 records · Page 2Linked to original sources

PubMed1983

Effects of ionizing radiation on nitric oxide myoglobin. Part 1. Effects on the NO-haem moiety.

Bovine nitric oxide myoglobin (NOMb) was irradiated with 40-4000 krad of gamma-radiation, and the effects on the haem studied using absorption spectroscopy and electron spin resonance (e.s.r.) spectroscopy. The results show the following behaviour. The bright red colour of NOMb changes to brown upon irradiation. This is similar to changes observed in radiation sterilized. nitrite-containing meats. NOMb becomes progressively denitrosylated, with met-myoglobin (metMb) as the immediate product. Upon increasing doses of radiation (up to 800 krad) at 0 degrees C parallel to NOMb denitrosylation, metMb is gradually converted, by water radiolytic products, to other products, believed to be ferromyoglobin and ferrimyoglobin peroxide. A minor quantity of 'choleglobin-type' pigments may also be formed at the highest doses. Freezing of NOMb has a substantial protective effect against radiation. Native bovine NOMb behaves as a pentaco-ordinate (hfs of 3 peaks with equal intensity); the bond between iron and N epsilon is thus dramatically stretched and weakened. Using a thermal energy analyser, no NO could be detected over irradiated NOMb solution, indicating rapid reaction of NO liberated from NOMb by radiation, with radiolytic products of water.

Animals↗

PubMed1983

Effects of ionizing radiation on nitric oxide myoglobin. Part 2. Effects on the globin moiety.

Irradiation of nitric oxide myoglobin (NOMb) induces changes in the haem as well as protein moiety of NOMb, especially at doses of 400-800 krad. The changes in the protein include: Conformational changes, with apparent partial denaturation of globin alpha-helix as evidenced by circular dichroism. Preferential scission of the polypeptide chain and dimerization via covalent bond(s) as evidenced by SDS-polyacrylamide gel electrophoresis. Products with a spectrum of hydrodynamic volumes between those of the monomer and the dimer are also formed. The shift of NOMb pIs toward more acidic pHs (probably due to modification and/or destruction of basic amino acid residues by water radiolytic products) as evidenced by isoelectric focusing.

Animals↗

PubMed1978

Reactions between peroxidizing lipids and histidyl residue analogues: enhancement of lipid oxidation and browning by 4-methylimidazole.

As a part of our study on the interactions between peroxidizing lipids and the histidyl imidazole side-chain in simple, low-moisture model systems, 4-methylimidazole (4MI) was reacted with methyl linoleate (ML). This analogue was chosen to avoid interference from other functional groups in histidine (free base) or in proteins. Changes in the concentrations of lipid hydroperoxides, carbonyls, 4MI, and brown pigments were followed over a period of 24 days. The results indicate that 4MI exhibits significant prooxidative activity by reducing the induction period as well as by enhancing the formation of brown pigments. These effects are more pronounced at high 4MI/MI molar ratios and under basic pH's. Upon interactions with peroxidizing ML, as much as 44% of initially present 4MI was destroyed by the sixth day of incubation.

Drug Evaluation↗

PubMed1976

Free radical reactions of peroxidizing lipids with amino acids and proteins: an ESR study.

Free radical transfer from oxidizing methyl linoleate to amino acids and proteins was studied in dry model systems incubated for periods up to 20 days. Electron spin resonance was used to study free radical production. Free radicals were detectable in the amino acids lysine, arginine, histidine, tryptophan, and cysteine. Reduced glutathione and, to a limited extent, cystine also gave free radical signals. Free radicals produced in proteins primarily showed central singlet lines, attributable to carbon-centered radicals, with g= 2.004+/- 0.001. Sulfhydryl proteins also exhibited downfield shoulders at g approximately equal to 2.015 and 2.023 that were essentially identical to peaks observed in cysteine and reduced gluathione. The field positions of sulfur resonace in cysteine and proteins suggested a sulfur-oxygen complex rather than thiyl radicals.

Amino Acids↗

PubMed1975