[Risk factors and the course of myocardial infarction in elderly women].

AIM: to elucidate risk factors and special features of myocardial infarction (MI) in elderly women. MATERIAL AND METHODS: We included into the study 217 women aged 34 to 89 years who had Q-wave or non Q-wave MI and were admitted for treatment in the cardiology department. These patients were divided into two age groups - younger than 60 years (n=79, mean age 51.6+/-5.9 years) and more or equal 60 years (n=138, mean age 71.7+/-6.9 years). RESULTS: The following risk factors were more frequent among older women: hypertension (95.7 vs 89.9%), diabetes mellitus (32.2 vs 24%). Women aged <60 years more often had obesity (43.0 vs 26.8%), dyslipidemia (63.3 vs 42.8%), smoking (18.9 vs 0.7%), and premature menopause (12.8% vs 5.0%). Women aged <60 years had combinations of 3 or 4 risk factors. Coronary angiography was carried out in 34.2% of women aged <60 years and in 18.8% of older women. Women aged <60 years compared with older women more often had single vessel coronary artery stenosis (55.6 and 23.3%, respectively), whereas in women aged more or equal 60 years prevailed multivessel coronary artery involvement (22.2 and 42.3%, respectively). MI in elderly women was more often complicated by Killip class III-IV acute heart failure, arrhythmias, recurrent MI, and hemotamponade, while younger women (aged <60 years) more often had early postinfarction angina and Dressler syndrome.

Adenylosuccinate synthetase of the yeast Saccharomyces cerevisiae: purification and properties.

Adenylosuccinate synthetase (AS-synthetase) was purified from the yeast Saccharomyces cerevisiae. The purification procedure included chromatography on DEAE-cellulose, phosphocellulose, and heparin-agarose. The pH and temperature optima for the enzyme activity (7.0 and 35 degreesC, respectively) and also pH and thermostability of AS-synthetase were determined. The native form of the enzyme exists as a dimer. The Km values for IMP, GTP, and L-aspartate are 1.7, 0.16, and 6.7 mM, respectively. ATP cannot be used instead of substrate GTP, whereas 2'-dGTP and dd-GTP are able to substitute for GTP in the reaction. ITP also can be a substrate as an analog of GTP and as an analog of IMP. Two intermediates of purine nucleotide biosynthesis de novo, 5-amino-4-(N-succinocarboxamide)imidazole ribonucleotide (ASCIR) and 5-amino-4-carbamoyl-imidazole ribonucleotide (ACIR), inhibit AS-synthetase. Hydroxylamine and aspartate analogs also inhibit the enzyme. Effective binding requires a four-carbon-atom chain and unsubstituted amino group; the charge of the beta-carboxy group is not necessary. Comparison of primary structures and substrate specificity of yeast ASCIR- and AS-synthetases suggests independent origin of these proteins.

ADE6 gene of Saccharomyces cerevisiae yeast encoding formylglycinamidine-ribonucleotide synthetase. Cloning, sequencing, and analysis.

The ADE6 gene of Saccharomyces cerevisiae yeast encoding the enzyme formylglycinamidine-ribonucleotide (FGAM)-synthetase of de novo synthesis of purine nucleotides was cloned and sequenced. The gene encodes a protein consisting of 1358 amino acids. The flanking regions of 1208 (5') and 728 bp (3') were also sequenced. The nucleotide motif TGACTC inherent to the promotor regions of other purine genes of yeast was located (-276 bp) in the 5'-region of the gene. The amino acid sequence of the yeast FGAM-synthetase was found to contain repeats (Leu430-Ala620 and Pro810-Ile1000). Repeats of similar patterns of conserved amino acids were also detected in the structure of all other FGAM-synthetases. A homology of FGAM-synthetases with certain proteins of viruses from the Herpesviridae family was found.

[Glycine amide ribonucleotide synthetase (EC 6.3.4.13)--is aminoimidazole ribonucleotide synthetase (EC 6.3.3.1) from Saccharomyces cerevisiae]. / Glitsinamidribonukleotid-sintetaza (KF 6.3.4.13)--aminoimidazolribonukleotid-sintetaza (KF 6.3.3.1) Saccharomyces cerevisiae.

The bifunctional enzyme GAR-synthetase-AIR-synthetase (E2-E5) of the yeast Saccharomyces cerevisiae has been studied. The yeast strain with overproduction of E2-E5 has been obtained. The enzyme from this strain, E2-E5, has been purified and characterized. The protein is a dimer composed of two subunits with M(r) of 87 kDa. The pH and temperature optima, pH stability and thermostability for E2 and E5 have been determined. The kinetic constants for E2 and E5 have been estimated. E2 and E5 are active only in the presence of Mg2+. E5 is a K(+)-dependent enzyme as is E5 from other sources. AMP is a competitive (to ATP) inhibitor for E5; hence, in yeast cells the purine nucleotide biosynthesis de novo is regulated at the first and fifth steps. Partial chymotryptic digestion of the purified protein gives rise to two fragments with M(r) of about 40 and 46 kDa; and E2 activity remains, while that of E5 disappears in the process.

[Saccharomyces cerevisiae ADE12 gene, coding for adenylosuccinate synthetase (EC 6.3.4.4). Cloning, sequencing, expression, and superproduction]. / Gen ADE12 drozhzhei Saccharomyces cerevisiae, kodiruiushchii adenilosuktsii-sintetazu (KF 6.3.4.4). Klonirovanie, sekvenirovanie, izuchenie ékspressii, superproduktsiia.

The cloning and sequencing of Saccharomyces cerevisiae ADE12 gene encoding the structure of adenylsuccinate synthetase (ASS) are reported for the first time. Comparative analysis of all known ASS sequences was carried out. Regulation of ADE12 gene expression by exogenic adenine was carried out. The properties of ASS which was isolated and purified from overproducing yeast strain were examined.