ABSTRACT
The role of reamberin, a succinate-containing infusion preparation in correlation of pulmonary metabolic and respiratory disturbances in patients with obstetric puerperal sepsis was estimated. The prospective randomized study enrolled 43 patients with puerperal obstetric sepsis complicated by polyorganic deficiency (SOFA 8-10). Nineteen patients of the 1st group and 24 patients of the 2nd group were additionally treated with reamberin in a dose of 800 ml/day for 8 days. The venous and arterial difference by glucose, lactate, pyruvate, diene conjugates, malondialdehyde and ceruloplasmin was investigated. The blood gases were determined with the Ciba Corning 45 apparatus. Lower metabolic activity of the lungs with prevalence of the glucose anaerobic metabolism and lower activity of the intrapulmonary antioxidant protection were observed in the patients with obstetric sepsis. The use of reamberin in the complex therapy of obstetric sepsis promoted maintenance of the initial balance and anaeroibic and aerobic pulmonary metabolism, thus providing shorter terms of the decompensation and recovery of the lungs respiratory function.
Subject(s)
Lung , Meglumine/analogs & derivatives , Puerperal Infection/etiology , Respiratory Distress Syndrome/drug therapy , Sepsis/drug therapy , Succinates/administration & dosage , Bacterial Infections/complications , Blood Glucose/analysis , Ceruloplasmin/analysis , Female , Humans , Lactates/blood , Lung/metabolism , Lung/physiopathology , Malondialdehyde/blood , Meglumine/administration & dosage , Pregnancy , Pyruvates/blood , Respiratory Distress Syndrome/etiology , Sepsis/complications , Sepsis/surgeryABSTRACT
Interaction of the Tramtrack protein from Drosophila melanogaster with DNA was analyzed by a cross-linking method. Tramtrack residues cross-linkable to the partially depurinated DNA were identified by direct sequencing. The N-terminal alpha-amino group of the protein DNA-binding domain was found to be the major product of cross-linking. The location of the N terminus on the DNA was determined by identification of the DNA bases that were cross-linked to the protein alpha-amino group. We conclude that accessory N-terminal peptide preceding the first zinc finger of Tramtrack directly interacts with DNA, both in specific and nonspecific DNA-protein complexes. Our finding explains the role in the protein binding of the DNA bases outside of the direct interaction with the zinc fingers.
Subject(s)
DNA-Binding Proteins/metabolism , DNA/metabolism , Drosophila Proteins , Drosophila melanogaster , Repressor Proteins/chemistry , Repressor Proteins/metabolism , Amino Acid Sequence , Animals , Base Sequence , Binding Sites , Cross-Linking Reagents/metabolism , DNA/chemistry , DNA-Binding Proteins/chemistry , Exonucleases/metabolism , Protein Binding , Protein Structure, Tertiary , Substrate Specificity , Trypsin/metabolism , Zinc FingersABSTRACT
Along with symmetrical features (palindromes, direct and inverted repeats), periodicities in the disposition of nucleotides in the origin of chromosome replication oriC from E. coli were studied by means of Fourier analysis. Peaks corresponding to the periods T = 2, 17, 95-100 nucleotides are the highest in the Fourier spectrum of oriC. Peaks corresponding to the periods T = 3, 11, 19, 13, 24, 27, 28, 41, 79-81 nucleotides are also prominent, but not so high. Thus, the main periodicities of the oriC spectrum of are not multiple of the B-DNA sugar-phosphate backbone period, which destabilize DNA at oriC and contributes to the spontaneous unwinding of DNA. The differences between the Fourier spectrum of oriC and those of regions adjacent to oriC are demonstrated.
