Reconstruction of Purine Metabolism in Bacillus subtilis to Obtain the Strain Producer of AICAR: A New Drug with a Wide Range of Therapeutic Applications.

AICAR is a natural compound, an analogue and precursor of adenosine. As activator of AMP-activated protein kinase (AMPK), AICAR has a broad therapeutic potential, since it normalizes the carbohydrate and lipid metabolism and inhibits the proliferation of tumor cells. The synthesis of AICAR inBacillus subtiliscells is controlled by the enzymes of purine biosynthesis; their genes constituting purine operon (pur-operon).

Carboxypeptidase from Streptomyces bikiniensis: primary structure, isolation, and properties.

A metallocarboxypeptidase produced by Streptomyces bikiniensis 27 strain (VKPM Ac-1783) (CPSb) was purified and characterized. The enzyme cleaves both basic and hydrophobic C-terminal amino acid residues from synthetic peptides, that is, it possesses specificity of mammalian carboxypeptidases A and B. The enzyme also hydrolyzes peptides bearing glutamic acid at the C-end.

Use of low volatility mobile phases in electroosmotic thin-layer chromatography.

A variant of electroosmotic thin-layer chromatography is suggested with the use of low volatility compounds as mobile phases aimed at drastically decreasing the evaporation of the mobile phase and improving the reproducibility of the method. The linear movement velocity of zones of separated compounds is experimentally shown to increase 2-12-fold in electroosmotic chromatography (compared to similar values in traditional TLC). The separation efficiency is also considerably increased.

B-Z transition in poly(dG-dC).poly(dG-dC) in the presence of formaldehyde amino derivatives.

It was shown by circular dichroism that the B-Z transition of poly(dG-dC).poly(dG-dC) in high NaCl concentrations occurred more rapidly in the presence of formaldehyde and Tris. The product of formaldehyde and glycine interaction induces changes in the poly(dG-dC).

Nuclear magnetic resonance of nucleotide-amidates. Investigation of the secondary structure of methylester of deoxyadenylyl-(5'-3')-deoxyadenylyl-(5' leads to N)-L-phenylalanine.

The secondary structure of methyl ester of deoxyadenylyl- - (5' - 3') - deoxyadenylyl - (5' leads to N) - L-phenylalanine / L- PheOMe - d(pApA)/ was investigated using proton magnetic resonance. The folded conformation stabilized by hydrophobic interactions in aqueous solution was shown for this compound. The investigation of the chemical shifts of aromatic protons of L- PheoOMe - d(pApA) permitted us to construct the conformational model of this compound.