[Characteristics of mRNA and cDNA of fructose-1,6-diphosphate aldolase]. / Kharakteristika mRNK i kDNK fruktozo-1,6-difosfatal'dolazy.

Problems concerning synthesis of fructose-1,6-diphosphataldolase A (EC 4.1.2.13) in vitro, and localization in a cell and sizes of mRNA of this enzyme are considered in the review. The following items are described: methods for production and properties of individual mRNA and cDNA of the aldolase isoenzymes; making of the amino acid sequence of the aldolase isoenzyme forms according to the nucleotide sequence of mRNA and cDNA and peculiarities of isoform structure in different tissues of animals; structure of mRNA and cDNA of FDP-aldolase in the norm and under pathology and mechanisms of the appearance of nonspecific enzyme isoforms. Regulation of protein biosynthesis under pathology is considered as exemplified by mRNA and cDNA of FDP-aldolase.

[Structural differences of C-terminal fragment of the alpha-subunits of rabbit muscle aldolase in normal animals and in experimental atherosclerosis]. / O strukturnykh razlichiiakh C-kontsevogo fragmenta al'fa-sub"edinitsy al'dolazy myshts krolikov v norme i pri'eksperimental'nom ateroskleroze.

The COOH-terminal BrCN fragment of the aldolase alpha-subunit from muscles of rabbits in norm and under atherosclerosis was studied by the method of dansyl-fingerprints in a silicagel and polyamide thin layer. It is shown that under atherosclerosis the amount of peptides in the fragment under study increases and the topography of two of them changes. The content of lysine, serine and valine enhances in it. The results evidence for structural differences in C-terminal fragment of aldolase alpha-subunits in muscles of rabbits in norm and under experimental atherosclerosis.

[Amino acid composition and subunit structure of rabbit muscle aldolase in experimental atherosclerosis]. / Aminokislotnyi sostav i sub"edinichnaia struktura al'dolazy iz myshts krolikov v usloviiakh éksperimental'nogo ateroskleroza.

Under atherosclerosis the fractions corresponding to alpha-subunits are focused at a more alkaline pH than the same fractions in the norm. The curve of the enzymic activity of the fractions with atherosclerosis is higher. beta-subunits of aldolase from muscles of intact rabbits and those with sclerosis are identical in the amino acidic composition. In the enzyme alpha-subunits under conditions of atherosclerosis the content of lysine, serine, glycine, valine gets higher. On the basis of the previous research which reveals peptide having no analogs in the norm in the C-terminal fragment of aldolase molecule an assumption is advanced that under conditions of atherosclerosis the intermediate C-terminal site of the enzyme alpha-chain changes.

[Structure of cytoplasmic glycerol-3-phosphate dehydrogenase in experimental atherosclerosis in rabbits]. / O strukture tsitoplazmaticheskoi glitserol-3-fosfatdegidrogenazy pri éksperimental'nom ateroskleroze krolikov.

Differences in the ratio of molecular forms of crystalline glycerol-3-phosphate dehydrogenase (GPD, EC 1.1.1.8) from sceletal muscle and in their primary structure were found in rabbits with experimental atherosclerosis as compared with normal animals. In atherosclerosis the molecular weight of GPD and of its fragments was increased; the amino acid composition of these GPD molecules differs from that of control rabbits as shown by estimation of content of 8 amino acids. Experimental atherosclerosis is apparently related to alteration in the GPD primary structure.