Biomedical subjects

E G Sarkisova

Publications and source records attributed to E G Sarkisova.

4 recordsLinked to original sources

PubMed2002

[Activity of pleural fluid adenosine deaminase in tuberculous pleurisy].

Examining the activity of adenosine deaminase in the pleural fluids of 69 patients with tuberculous pleurisy of various etiology from the clinics of Armenia indicated that it was greater than the threshold value of 20 U/L in 95.7 of 47 patients with tuberculous pleurisy. The specificity of this parameter for this disease was 0.91. The prognostic value of the test with positive and negative results was 0.96 and 0.94, respectively. The diagnostic value of the ADA test was 0.94.

Adenosine Deaminase↗

PubMed1987

[The role of tryptophan residues of NADPH-adrenodoxin reductase in the formation of complex with adrenodoxin].

Chemical modification of tryptophan residues by N-bromosuccinimide was used to determine the role of these residues in the NADPH-adrenodoxin-catalyzed reduction of adrenodoxin, dichlorophenolindophenol and ferricyanide. It was shown that the rate of reduction of all electron acceptors diminishes with modification of tryptophan residues. The most significant decrease of the enzyme activity is observed in case of adrenodoxin-catalyzed reactions. It was suggested that tryptophan residues are responsible for the adrenodoxin reductase interaction with adrenodoxin.

Adrenal Cortex↗

PubMed1976

[Adrenal cortex cytochrome c].

The method of preparation of highly purified cytochrome c from bovine adrenal cortex is described. Absolute spectra of the protein in reduced and oxidized states and some its physico-chemical properties are investigated.

Adrenal Cortex↗

PubMedDate not supplied

[Interaction of flavin adenine dinucleotide and tryptophan NADPH-adrenodoxin reductase complexed with adrenodoxin].

The NADPH-adrenodoxin complex with adrenodoxin is responsible for the transformation of the two-electron flow from NADH to the mono-electron flow to cytochrome P-450 in the steroid-hydroxyl enzyme system of mitochondria of kidney crust. Depolarization of emission of the reductase prosthetic group FAD with the maximum at 525 nm excited at the wave length approximately 290 nm in comparison with the excited at 450 nm provides an evidence of presence of the Ferster energy excitement transfer to FAD from the group absorbed at 290 nm. This fact and the form of absorbance spectra of the complex of two peptide points to the fact that the complex formation is accompanied by interaction of FAD with the residue of tryptophan in the reductase. Based on these facts and the data concerning participation of tryptophan and tyrosine of adrenodoxin in the electron transfer between the hypothesis is suggested about the intracomplex path of the electron that can explain the mechanism of switching of the two-electron transfer into the mono-electron one.

Adrenal Cortex↗