Staged equilibrium of carbonic anhydrase unfolding in strong denaturants

It has been shown by 1H-NMR, circular dichroism, fluorescence and viscometry techniques that equilibrium unfolding of carbonic anhydrase B (a one-domain globular protein) in urea guanidine hydrochloride consists of two sequential stages. The first stage is connected with a decrease of intramolecular interactions, stabilizing the rigid tertiary structure and with the increase of mobility of aliphatic side chain groups. At the second stage the decrease of protein secondary structure and hydrophobic interactions take place as well as the increase of mobility of massive aromatic side chain groups.     

The biological effects in animals related to the accident at the Chernobyl Atomic Electric Power Station. 2. The state of bone marrow hematopoiesis in rats]

It has been shown that rats born during the first months after the Chernobyl A.P.S. disaster exhibit essential changes in the peripheral blood and bone marrow haemopoiesis throughout the entire lifetime. Rats brought up in Chernobyl from the age of three months on display even more pronounced changes. It is assumed that the changes in the haemopoiesis develop due to the continuous influence of low-level radiation of different quality and are attributed to the effect of the incorporated radionuclides.     

Dynamics and ultrastructural characteristics of osteoclast formation

Using electron microscopy and 3H-thymidine autoradiography it has been shown that osteoclasts of rats and rabbits are formed by fusion of cell precursors which become members of the osteoclasts 14 hours following S-phase. Monoblasts and promonocytes are considered as DNA-synthesizing forms. A single injection of parathormone in a dose of 10 units/100 g of body weight leads to an increase in the fractions of DNA-synthesizing cells. Monocytes and macrophages appear to be direct osteoclast precursors in resorption zones. As a result of their fusion there appear "unfixed" polynuclear macrophages (young osteoclasts). The number of osteoclast nuclei increases also at the expense of little-differentiated phagocytes, the inclusion of the latter takes place at different stages of the life span of osteoclasts depending on the intensity of bone resorption processes. The structural characteristics of fusion of cell precursors are considered.     

Submicroscopic changes in the capillary cells of an area of osteogenesis during body uptake of lead acetate

Ultrastructurometry has revealed that daily entry of lead acetate in a dose of 50-100 mg/kg per body weight for 1-2.5 months increases chromatin condensation in nuclei, promotes swelling and myelin-like degeneration of the mitochondria, hyperplasia of the endoplasmic net, as well as appearance of the "enlightment" zones in the cytoplasm of endotheliocytes and perivascular cells of the capillaries from a metaphyseal zone of the rat femur. These changes are a consequent of the edema of cells and of the decrease in their biosynthetic activity.     

Ultrastructural characteristics of osteoclasts in different functional states

By electron microscopy and autoradiography, a study was made of osteoclasts in the metaphyseal zones of the femora of 1-7-day old rabbits and rats. It was established that depending on the intensity of resorptive processes osteoclasts noticeably differed in their morphology (shape, size, number of nuclei, degree of development of intracellular organelles, "brush border"), as well as in the level of biosynthetic activity registered by incorporation intensity of 3H-uridine and 3H-methionine in these. According to these indices, osteoclasts were classified as young, mature functionally active, and non-active osteoclasts, as well as perishing ones. The defined morpho-functional states represent successive stages of the life cycle of osteoclasts.     

Site-specific enzymatic cleavage of TMV RNA directed by deoxyribo- and chimeric (deoxyribo-ribo)oligonucleotides

The TMV RNA molecule can be cleaved at a single site by RNase H directed by chimeric oligo(deoxyribo-ribo)nucleotide with an internucleotide pyrophosphate bond.     

A novel peptide recognition mode revealed by the X-ray structure of a core U2AF35/U2AF65 heterodimer

U2 auxiliary factor (U2AF) is an essential splicing factor that recognizes the 3' splice site and recruits the U2 snRNP to the branch point. The X-ray structure of the human core U2AF heterodimer, consisting of the U2AF35 central domain and a proline-rich region of U2AF65, has been determined at 2.2 A resolution. The structure reveals a novel protein-protein recognition strategy, in which an atypical RNA recognition motif (RRM) of U2AF35 and the U2AF65 polyproline segment interact via reciprocal "tongue-in-groove" tryptophan residues. Complementary biochemical experiments demonstrate that the core U2AF heterodimer binds RNA, and that the interacting tryptophan side chains are essential for U2AF dimerization. Atypical RRMs in other splicing factors may serve as protein-protein interaction motifs elsewhere during spliceosome assembly.