Biomedical subjects

T A Zhilina

Publications and source records attributed to T A Zhilina.

4 recordsLinked to original sources

PubMed1988

[Interaction of muscle glycogen phosphorylase b with riboflavin, its tetraacetyl derivative and their analogs].

The interaction of rabbit skeletal muscle glycogen phosphorylase b with riboflavin, 2',3',4',5'-tetraacetylriboflavin and their analogues, containing different substituents in the positions 6, 8 and 8 alpha, has been studied. Dissociation constant for the complex of the enzyme and riboflavin was determined to be 12.5 microM (pH 6.8; 20 degrees C) by sedimentation velocity method. Riboflavin and its analogues have been found to inhibit glycogen phosphorylase b. The inhibitor half-saturation concentration values increase in the following order: riboflavin (18 microM), 8-methoxy(nor)rifoblavin (23 microM), 8 alpha-bromo-2',3',4',5'-tetraacetylriboflavin (40 microM), 6-bromoriboflavin (40 microM), 8 alpha-hydroxyriboflavin (60 microM), 8-hydroxy(nor)riboflavin (90 microM), 8 alpha-(gamma-carboxypropylamino-2',3',4',5'-tetraacetylriboflav in (90 microM), 8 alpha-[p-(5-ethyl-1,3,4-thiodiazol-2-ylsulfamido)phenylamino ]- 2',3',4',5'-tetraacetylriboflavin (100 microM), 8 alpha-(L-methionyno)-2',3',4',5'-tetraacetylriboflavin (120 microM), 8 alpha-[p-(thiazol-2-ylsulfamido)phenylamino]- 2',3',4',5'-tetraacetylriboflavin (140 microM), 8 alpha-(p-sulfamidophenylamino)-2',3',4',5'-tetraacetylriboflavi n (180 microM), 8 alpha-(p-carboxyphenylamino)-2',3',4',5'-tetraacetylriboflavin+ ++ (210 microM), 2',3',4',5'-tetraacetylriboflavin (250 microM), 8 alpha-(L-homoserino)-2',3',4',5'-tetraacetylriboflavin (340 microM), 8 alpha-(L-glutamo)-2',3',4',5'-tetraacetylriboflavin (360 microM). The existence of glycogen phosphorylase b complexes with riboflavin and its analogues has been proved by methods of absolute and difference spectrophotometry.

Animals↗

PubMed1985

[Interaction of muscle glycogen phosphorylase B with flavin-adenine dinucleotide and its analogs].

The inhibition of rabbit skeletal muscle glycogen phosphorylase b by FAD and its analogues with substitutes in the position 8 has been studied. The value of half-saturation, [I]0,5, for inhibitors increases in the following order: FAD (44 microM), 8 alpha-hydroxy-FAD (60 microM), 8-dimethylamino (nor)-FAD (69 microM), 8 alpha-(N-acetyl-L-cystein-S-yl)-FAD (106 microM). From the comparison of these values with those obtained earlier for FMN analogues, it follows that in the case of FAD the half-saturation value is less sensitive to modification of the position 8 in the flavin isoalloxazine ring. The existence of the glycogen phosphorylase b FAD-complex has been proved by the spectrophotometry and sedimentation methods. The positions of maxima of optical absorption of the enzyme-bound FAD in the 300-500 nm region are identical with corresponding positions for FMN. FAD has been shown to hinder the AMP-induced transition of dimeric form of the enzyme to tetrameric one.

Animals↗

PubMed1984

[Interaction of muscle glycogen phosphorylase B with flavin mononucleotide and its analogs].

The inhibition of rabbit skeletal muscle glycogen phosphorylase B by FMN and its analogues with substituents in the positions 6 and 8 has been studied. Inhibiting action of FMN is manifested in reducing the limiting rate of enzymic reaction and in increasing the half-saturation concentration of AMP. The inhibitor half-saturation values (in microM) increase in the following order: FMN (13,5), 6-bromo-FMN (27), 8 alpha-hydroxy-FMN (30), 8-dimethylamino(nor)-FMN (33), 6-(N-acetyl-L-cysteine-S-yl)-FMN (44), 6-amino-FMN (96), 8-hydroxy(nor)-FMN (109), 6-nitro-FMN (170), 8 alpha-(N-acetyl-L-cysteine-S-yl)-FMN (260). The existence of the glycogen phosphorylase B complexes with FMN or its analogues has been proved by spectrophotometry and sedimentation in analytical ultracentrifuge. FMN has been shown to hinder AMP-induced transition of dimeric form of the enzyme to tetrameric one. AMP at high concentrations has been found to inhibit glycogen phosphorylase B.

Animals↗

PubMed1977

8alpha-hydroxyflavinmononucleotide and related compounds.

2', 3', 4'-Triacetyl-FMN has been transformed by selective radical bromination into 2', 3', 4'-triacetyl-8alpha-bromo-FMN, and the following hydrolysis of the latter has afforded 8alpha-hydroxy-FMN. The presence of the hydroxy group in the 8alpha position of 8alpha-hydroxy-FMN is confirmed by its acetylation into 2', 3'-diacetyl-8alpha-acetoxyriboflavin-4', 5'-cyclophosphate. The absorption spectra of the synthesized compounds have shown the reduction of the extinction ratios of the first and second absorption maxima in comparison with the extinction of the same maxima for 8alpha-hydroxyriboflavin. Unlike FMN, fluorescence quenching for 8alpha-hydroxy-FMN has been found.

Flavin Mononucleotide↗