Biochemistry. Biokhimii︠a︡.
Publisher:
Consultants Bureau [etc.]. Moscow : MAIK Nauka/Interperiodica (2007)
Country: United States
Language: English
Author(s):
Consultants Bureau.
Start Year:1956 -
ISSN:
0006-2979 (Print)
1608-3040 (Electronic)
0006-2979 (Linking)
1608-3040 (Electronic)
0006-2979 (Linking)
Impact Factor
2.8
2022
| NLM ID: | 0376536 |
| (OCoLC): | 01536397 |
| (DNLM): | B15200000(s) |
| LCCN: | 59-29619 |
| Classification: | W1 BI64 |
Intermediate amyloid oligomers of lysozyme: Is their cytotoxicity a particular case or general rule for amyloid? In the current study we investigated the molecular mechanisms of cytotoxicity of amyloid oligomers of horse milk lysozyme. We have shown that lysozyme forms soluble amyloid oligomers and protofibrils during incubation at pH 2.0 and 4.5 and 57 degrees C. These structures bind the amyloid-specific dyes thioflavin T and Congo Red, and their morphology and size were analyzed by atomic force microscopy. Monomeric lysozyme and its fibrils did not affect the viability of three cell types used in our experiments including primary murine neurons and fibroblasts, as well as neuroblastoma cell line IMR-3...
Mechanism of oxidation of oxymyoglobin by copper ions: comparison of sperm whale, horse, and pig myoglobins. The influence of Cu2+ concentration, pH, and ionic strength of the solution as well as redox-inactive zinc ions on the rate of oxidation of sperm whale, horse, and pig oxymyoglobins (oxy-Mb) by copper ions has been studied. These myoglobins have homologous spatial structures and equal redox potentials but differ in the number of histidines located on the surface of the proteins. It was shown that oxy-Mb can be oxidized in the presence of Cu2+ through two distinct pathways depending on which histidine binds the reagent and how stable the complex is. A slow pH-dependent catalytic process is obse...