Tag Archives: hemoglobin

The contribution of Nobel prize laureates to research of the protein structure: J. Sumner, J. Northrop, W. Stanley, L. Pauling, F. Sanger, M. Perutz, J. Kendrew

V. M. Danilova, R. P. Vynogradova, S. V. Komisarenko

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: valdan@biochem.kiev.ua

Received: 11 Match 2020; Accepted: 15 May 2020

The second half of the 20th century was marked by remarkable discoveries in the chemistry and biochemistry of proteins, in particular, in establishing the protein structure. James Sumner, John Northrop, and Wendell Stanley, the Nobel Laureates in chemistry in 1946, were the first to isolate individual enzymes and viruses in a pure crystalline form and prove their protein nature, thereby making an invaluable scientific contribution to the development of important biological disciplines such as biochemistry, enzymology, virology, and molecular biology. A significant contribution to understanding chemical bonding in the formation of the different levels of a protein structure was made by Linus Pauling – a prominent American scientist of the 20th century. He was awarded the Nobel Prize in Chemistry in 1954 “for his research into the nature of the chemical bond and its application to the elucidation of the structure of complex substances”. Biochemists know him well as the author of the secondary structure of proteins – the α-helix and the β-sheet. Frederick Sanger, a two-time Nobel Prize winner (1958 and 1980), was the first among researchers who determined the primary amino acid sequence of a protein, for example, of two insulin polypeptide chains A and B. F. Sanger proved that the sequence nature of proteins’ structures is analogous to that of gene sequences in the DNA, and thus, the same principles may be applied. The difficult question of how a protein molecule is arranged in space was answered by the English biochemists Max F. Perutz and John C. Kendrew. They determined the three-dimensional structure of hemoglobin and myoglobin proteins by X-ray diffraction and were awarded the Nobel Prize in Chemistry in 1962 “for their studies of the structures of globular proteins”.

Oxygen binding by marine fish blood under hypothermic experimental conditions

A. A. Soldatov1, I. A. Parfyonova2

1Institute of Biology of Southern Seas, National Academy of Science of Ukraine, Sevastopol;
e-mail: alekssoldatov@yandex.ru;
2Sevastopol National Technical University, Ukraine

Influence of temperature in the range of 1-15 °С on oxygen binding properties of blood of thermophilic – golden mullet (Liza aurata), anchovy (Engraulis encrasicolus), and cold-tolerant – sardelle (Clupeonella cultriventris) fishes has been investigated under experimental conditions. Heat dependence of oxygenation reaction in thermophilic fish blood at temperature below 10 °C considerably increases, which is evidenced by high ΔH values. That is accompanied by a substantial increase of blood oxygen affinity and complicates blood deoxygenation at the tissue level. This reac­tion is apparently determined by the change of hemoglobin interaction with intraerythrocyte medium. The concentration of NTP in erythrocytes increases, that partially compensates negative changes of blood oxygen affinity (parameter P50 is raised) under long-term maintenance of fishes at 5 °С. However this reaction is not observed at low temperatures (1-2 °C).

Biochemical changes in rats under the influence of cesium chloride

N. M. Melnikova, O. V. Yermishev

National University of Life and Environmental Sciences of Ukraine, Kyiv;
e-mail: iermishev@i.ua

Cesium is lately accumulated actively in the environment, but its influence on human and ani­mal organism is the least studied among heavy metals. It is shown that the action of cesium chloride in rats caused significant changes in blood chemistry, which are characterized by a decrease of total protein content, pH, an increase in the level of urea, creatinine, glucose and total hemoglobin. The results showed that potassium content in all the studied organs and tissues of poisoned rats decreases under the action of cesium chloride. Histological examination of the heart tissue in rats poisoned with cesium chloride indicates the onset of pathology of cardiovascular system. It was found out that use of the drug “Asparkam” reduces the negative effect of cesium chloride on the body of rats.