Comparative Stability Assessment of Laccases from the Basidiomycetes Coriolus hirsutus and Coriolus zonatus in the Presence of Effectors

Stability characteristics of the laccases of the basidiomycetes Coriolus hirsutus and Coriolus zonatus were measured comparatively at temperatures of 25 and 40°C in the presence of various effectors (proteins, salts, polyalcohols, polyacids, and polyelectrolytes). Stabilization effects of cations on the laccases from C. hirsutus and C. zonatus decreased in the descending series Cu²⁺ > Mg²⁺ > Ca²⁺ and Ca²⁺ > Mg²⁺ > Mn²⁺, respectively. Tween 20 caused insignificant stabilization of the two enzymes. The C. zonatus laccase was also insignificantly stabilized as a result of treatment with bovine serum albumin. The enzymatic activity of the laccase preparations from C. hirsutus and C. zonatus was conserved virtually completely after vacuum drying (84 and 93%, respectively). The most effective stabilizer of the C. hirsutus laccase was found to be dextran (17 kDa). Dry preparations treated with this agent conserved up to 95% of the enzymatic activity. The most effective stabilizer of the C. zonatus laccase was polyacrylic acid (102% of the initial activity).     

Menaquinone function in the respiratory chain of Micrococcus lysodeikticus]

Menaquinone-9 which is destructed under long-wave UV-irradiation is isolated from Micrococcus lysodeikticus membranes. NAD-H, malate and lactate oxidases are observed to be inhibited under irradiation, dehydrogenases of these substrates being almost intact. Photoinactivation of menaquinone results in the reduction of only one from two cytochromes b, presented in the membrane, thus testifying the location of menaquinone-9 between cytochromes b in the respiratory chain. Reconstruction of malate, NAD-H and lactate oxidases after irradiation took place when natural menaquinone (MQ-9) or menadione (MQ-0) were added. Detailed scheme of M. lysodeikticus respiratory chain is given.     

Interactions between dopamine, serotonin, and other reward factor

Interactions between dopamine, serotonin, reward factors, and main representatives of regulatory peptide families have been analyzed using the bulk of disembodied publications of the last 50 years. A database covering the direction of physiological effects, doses, and administration modes of regulatory peptides and biologically active compounds, species, organ and tissue systems, as well as receptor mechanisms has been created. Complex cascade interactions between dopamine, serotonin, reward factors, and regulatory peptides were analyzed and organized. Analysis of coordinated functioning of the dopaminergic and serotonergic systems (at different levels) allowed us to reveal their opponent reciprocal interactions and to introduce their integral characteristics.     

Changes in peroxidation under conditions of 3,4-benzypyrene-induced carcinogenesis

The activities of enzymatic systems generating and destroying peroxides and the lipid peroxide content in neoplastic rat liver and 3,4-benzpyrene-induced sarcoma were studied. The tumour was characterized by high activity of glutathione peroxidase and low activity of catalase. No urate- and glycolate oxidases or ascorbat dependent peroxidation of lipids and lipid peroxides were found in the tumour. In the liver of neoplastic animals the activities of glutathione peroxidase and NADPH-dependent system of microsomal phospholipid peroxidation and the lipd peroxides content were increased, whereas the activities of catalase and urate oxidase were decreased.     

Intracellular proteolysis: Signals of selective protein degradation

Selective proteolysis is one of the mechanisms for the maintenance of cell homeostasis via rapid degradation of defective polypeptides and certain short-lived regulatory proteins. In prokaryotic cells, high-molecular-mass oligomeric ATP-dependent proteases are responsible for selective protein degradation. In eukaryotes, most polypeptides are attacked by the multicatalytic 26S proteasome, and the degradation of the majority of substrates involves their preliminary modification with the protein ubiquitin. The proteins undergoing the selective proteolysis often contain specific degradation signals necessary for their recognition by the corresponding proteases. This article is dedicated to the 25th Anniversary of the journal Bioorganicheskaya Khimiya