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Stanislaw J. Przylecki

75%
Acetylcholinesterase (AChE) sequentially extracted from mature specimens of Hymenolepis diminuta was shown to be a globular protein, the monomeric form of which (Ga₁) had molecular mass of 66 kDa as determined by SDS-PAGE. Amphiphilic character of the enzyme was revealed by Triton X-l14 phase partitioning. The cestode AChE preferred acetylthiocholine over propionyl- and butyrylthiocholine as substrate, split N-acetyl-ß-methylthiocholine and myristoylcholine but did not hydrolyze ß-carbonaphthoxycholine, a substrate for butyrylcholinesterases. It was sensitive to 10⁻⁵ M physostigmine and 10⁻⁵ M BW284C51 but not to 10⁻³ M iso-OMPA. No butyrylcholinesterase activity was detected in extracts from the parasite.
The immunological, haematological and biochemical analyses of blood plasma in bitches with 50 days lasting induced zearalenone micotoxicosis were carried out. It can be indirectly suggested that the inhibition of the humoral reaction of the organism, stimulation of detoxification effect in the liver and decreased cellular answer took place.
G-protein coupled receptors (GPCRs) are thought to be proteins with 7-membered transmembrane helical bundles (7TM proteins). Recently, the X-ray structures have been solved for two such proteins, namely for bacteriorhodopsin (BR) and rhodopsin (Rh), the latter being a GPCR. Despite similarities, the structures are different enough to suggest that 3D models for different GPCRs cannot be obtained directly employing 3D structures of BR or Rh as a unique template. The approach to computer modeling of 7TM proteins de­veloped in this work was capable of reproducing the experimental X-ray structure of BR with great accuracy. A combination of helical packing and low-energy conformers for loops most close to the X-ray structure possesses the r.m.s.d. value of 3.13 Ä. Such a level of accuracy for the 3D-structure prediction for a 216-residue protein has not been achieved, so far, by any available ab initio procedure of protein folding. The approach may produce also other energetically consistent combinations of helical bundles and loop con- formers, creating a variety of possible templates for 3D structures of 7TM proteins, in­cluding GPCRs. These templates may provide experimentalists with various plausible op­tions for 3D structure of a given GPCR; in our view, only experiments will determine the fi­nal choice of the most reasonable 3D template.
Cysteine proteases (CPs) are responsible for many biochemical processes occurring in living organisms and they have been implicated in the development and progression of several diseases that involve abnormal protein turnover. The activity of CPs is regulated among others by their specific inhibitors: cystatins. The main aim of this review is to dis­cuss the structure-activity relationships of cysteine proteases and cystatins, as well as of some synthetic inhibitors of cysteine proteases structurally based on the binding frag­ments of cystatins.
The influence of iodine-iodide solution on (he biochemical and immunological properties of human thyroglobulin (hTg) were studied. Human Tg preincubated with the iodine-iodide solution is split to small molecular mass fragments after disulphide bridge reduction with dithiothreitol. The peptide bond cleavage by iodine pretreatment and reduction is possibly linked with the coupling reaction of diiodotyrosyl residues. Pretreatment of hTg with iodine-iodide solution at 1 -10 |iM decreased the binding of autoantibodies to hTg. The iodine-iodide induced inactivation of hTg autoepitopes is pH dependent and is possibly caused by iodination of tyrosyl residues present in the epitope structure.
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Biochemistry of magnesium

63%
Magnesium is essential for biochemical functions of cells. Since Mg2+ has a relatively low ionic radius in proportion to the size of the nucleus (0.86 versus 1.14 f A for Ca2+), it shows exceptional biochemical activity. Due to its physicochemical properties, intracellular magnesium can bind to the nucleus, ribosomes, cell membranes or macromolecules occurring in the cell’s cytosol. It is indispensable for the nucleus to function as a whole and for the maintenance of physical stability as well as aggregation of rybosomes into polysomes able to initiate protein synthesis. Mg2+ can also act as a cofactor for ribonucleic acid enzymes (ribozymes) capable of specifically recognizing and cleaving the target mRNA. As an essential cofactor in NER, BER, MMR processes, Mg2+ is required for the removal of DNA damage. An activator of over 300 different enzymes, magnesium participates in many metabolic processes, such as glycolysis, Krebs cycle, β-oxidation or ion transport across cell membranes. Mg2+ plays a key role in the regulation of functions of mitochondria, including the control of their volume, composition of ions and ATP production.
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