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Biomedical subjects

S G Sharoian

Publications and source records attributed to S G Sharoian.

9 recordsLinked to original sources
PubMed1996

[The role of tryptophan in appearance of adenosine deaminase activity].

Chemical modification of tryptophan residues with N-bromosuccinimide and their photooxidation in the presence of trichloroethanol inhibited the activity of adenosine deaminase purified from gray and white matter of calf brain. Only two of six modified residues are important for enzyme activity. Preliminary kinetic data indicate that these essential tryptophan residues are adjacent to the substrate-binding site of the enzyme.

Adenosine Deaminase↗
PubMed1994

[Isolation, purification, and comparative study of the properties of adenosine deaminase from five regions of the cattle brain].

Adenosine deaminase from the white and gray matter of the large hemispheres, cerebellum, medulla oblongata and pituitary anterior lobe has been isolated and purified. The pH optimum, Km, molecular mass, yield and specific activities for all the enzyme preparations have been determined. Gel filtration and electrophoresis data point to the heterogeneity of the enzyme. The lack of effects of SH-reagents suggests the absence of an essential SH-group. Among five bivalent metal ions, only Cu2+ irreversibly inhibited the enzyme activity in all the preparations.

Adenosine Deaminase↗
PubMed1976

[Soluble cerebral metalloproteins. II. Superoxide dismutases of cerebral gray and white matter].

Superoxide dismutases (SOD) of high purity have been obtained from grey and white matter of bovine brain cerebral hemispheres. The SOD obtained have been shown to have three isoenzymes (a, b, c). A study of the catalytic and macromolecular properties of the SOD obtained from grey and white matter of cerebral hemispheres as well as their optical and electron paramagnetic resonance spectra indicates that both proteins possess similar properties. The possible function of SOD in grey and white matter of brain is discussed.

Animals↗
PubMed1975

[Soluble cerebral metalloproteins. 1. Purification and properties of cerebral cortex cytochrome c].

Cytochrome c from grey matter of brain has been obtained as a homogeneous preparation by electrophoresis on polyacrylamide gel and following electrofocusing in ampholine solutions. Its molecular weight, content of iron, redox potential and isoelectric point have been established. The absolute spectra of its oxidized and reduced forms are presented. Cytochrome c of brain cortex is similar in its properties to that obtained from other animal tissues as the heart and adrenal cortex.

Animals↗