[Cardiovascular function in chronic alcoholic intoxication].
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Biomedical subjects
Publications and source records attributed to V A Iakovlev.
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Radioimmunochemical assay was used to study the hypophyseal and peripheral hormones activity in 60 patients with chronic alcoholism, stage II. A correlation has been established between the patient's age and prolactin and FSH concentrations, as well as between the duration of the recent hard drinking and the concentrations of prolactin, testosterone, FSH and interstitial cell stimulating hormone. It has been shown that the manifestation of the alcoholic abstinent syndrome depended on the prolactin concentration. The test sensitivity estimated by the prolactin level rise and the testosterone level reduction reached 92.3%. The specificity of the changes detected comprised 25%. A conclusion has been made that the disorders noted in the patients with chronic alcoholic intoxication can be used as an objective test in the alcoholism diagnosis.
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Two cases of Gaucher's disease of the juvenile type are described, in a boy of 1 year and 7 months and in a girl of 8 years. The juvenile type of Gaucher's disease is documented by detection in the internal organs of typical Gaucher's cells formed mainly of histiocytes and macrophages, PAS-positive and weakly positive with Sudan III, and by the absence of the brain gangliocytes impairments. The peculiarity of these cases consists in the combination of glucocerebroside with congenital developmental defects of the urinary system: in one case with bilateral megaureter and hydronephrosis and in the second one with developmental defect of the renal arteries and bilateral cystic renal dysplasia.
Hormone levels were examined in the venous blood in 54 men suffering from stage 2 alcoholism and in 30 normal subjects, using a radioimmunochemical assay. The alcoholics were found to have a statistically significant increase in prolactin and a decrease in testosterone. A definite ratio in the secretion of these hormones differing from that in the control group was elucidated. This ratio (prolactin-testosterone index) is proposed as a diagnostic test of alcoholism.
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The interaction of AdoCbl-dependent glycerol dehydratase with the substrates (glycerol, 1,2-propandiol, ethylene glycol) and their analogs (aliphatic diols) was studied kinetically. It was found that all the diols tested are competitive inhibitors of the enzyme with respect to substrates. The arrangement of hydroxyl groups in the molecule, the length of the carbohydrate chain and the nature of the substituent at the C-3 atom are essential for the binding of diol in the active center. The ternary enzyme-AdoCbl-substrate (analog) complexes are subjected to specific inactivation at a rate, which depends on the chemical structure of the substrate (analog). The constants for inactivation and dissociation of the ternary complexes were determined. It was shown that in contrast to the double complexes (enzyme-AdoCbl), the inactivation of the ternary complexes does not depend on oxygen. Some aspects of the mechanism of specific inactivation of glycerol dehydratase are discussed.
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The interaction between 8 adenosyl cobalamine (AdoCbl) analogs modified in adenine and deoxyribose of the nucleoside ligand and glycerol dehydratase from Klebsiella pneumoniae ATCC 25955 was studied. It was found that araadenosyl-, 3-isoadenosyl-, aristeromycyl- and nebularyl cobalamines possess coenzymic properties. The catalytic activities of these analogs complexes with glycerol dehydratase make up to 110, 36, 30 and 6% of the enzyme activity with the natural cofactor AdoCbl. Benzimidazolribosyl-, toyokamycil-, L-adenosyl- and adenosylethyl cobalamines are effective competitive inhibitors with respect to AdoCbl. All AdoCbl analogs have high affinity for the apoenzyme; their Km and Ki values are close to 10(-7)--10(-8) M. The inactivation kinetics of catalytically active glycerol dehydratase complexes in the absence of substrate were studied. The rate of this process was found to depend on the structure of the analogs. It was shown that inversion of the 2'-OH-group of deoxyribose in AdoCbl results in the increase of Km for the substrate (1,2-propanediol). The main parameters of the CD spectra for AdoCbl analogs are described.
The 24-hour rhythm of values characterizing the elastic resistance of large arterial vessels and the arterial pressure was studied in 107 patients with hypertensive disease and in 79 normal persons by means of N.N. Savitsky's mechanocardiographic method. In healthy persons the hemodynamic values were marked by regular daily changes, while in those with hypertensive disease the daily rhythm of hemodynamics was considerably distorted, the degree and frequency of the disorder in the rhythm being dependent first and foremost on the severity of the disease. In patients with stage IB and stage IIA hypertensive disease a daily rhythm typical of a healthy person was retained, but the fluctuations in the values were of a higher level and range. The highest values of all indices were recorded in stages IIB and III and two variants of changes in the shape of the daily curve of arterial pressure and tone of arterial pressure were revealed; the first was characterized by the values being highest at night and in the early morning hours and lowest between 12 and 13 p.m., while the second, which was less frequent, corresponded to the shape of the daily curve peculiar to healthy persons.
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Effect of temperature, pH and univalent cation on kinetics of self-activation of B12-dependent glycerol dehydratase (GD) from Aerobacter aerogenes with Co alpha-[alpha-(5,6-dimethylbenzimidazolyl]-Co beta-adenosylcobamide (AdoCbl) was investigated. The activation energy of the process of GD inactivation is found to be 3.9 kkal/M, the effect of pH on GD inactivation being insignificant. Monovalent cation is not required for the formation of GD-AdoCbl complex, but it protects the complex from selfinactivation. The rate of GD inactivation greatly depends on concentration of monovalent cations. Effect of K+, Rb+, Cs+, Tl+ and NH4+ cations, which are enzyme cofactors, qualitatively differs from the effect of Na+ and Li+, which are inactive in a catalytic reaction. The presence of at least two cation-binding sites in GD molecule is suggested. Possible mechanism of the effect of environmental factors in self-inactivation of GD-AdoCbl complex is discussed.
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Hydrazide group of 4-substituted NAD analogues is shown to interact with functional groups of substrate-binding site in double complexes with pig muscle lactate dehydrogenase (isoenzyme M4). The lactic acid residue, which is structurally incorporated into NAD analogue, improves slightly the binding of dinucleotide, while 2,2,6,6-tetramethylpiperidine-1-oxyl residue considerably decreases the firmless of binding. The comparison of the inhibitory ability of oxamate, incotinic acid hydraxide and their spin-labelled derivatives indicates the restricted and stiff sizes of a substrate-binding site.
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