J. Planar Chromatogr. 17, 181-185 (2004). HPTLC of an inclusion complex of coenzyme Q10 with beta-cyclodextrin on silica gel by one-dimensional, two-dimensional, and multi-dimensional separation with 1) dioxane - water 1:1 and 2) chloroform - methanol 11:9. Detection by spraying with 5 % phosphomolybdic acid in ethanol and drying at 110 °C, followed by spraying with 50 % sulfuric acid and heating at 120 °C for 5 min.

J. Planar Chromatogr. 28, 333-336 (2015). HPTLC of glucose-6-phosphate and glucose-6-phosphate dehydrogenase (G6PDH) on silica gel previously dipped into 100 mM Tris-HCl buffer (pH 7.8) and activated at 110 °C for 40 min, with 100 mM Tris-HCl buffer (pH 7.8) containing coenzyme NAD+ with the desired concentration. Quantitative determination of NADH product by absorbance measurement at UV 340 nm. The method allowed on-plate assay of the G6PDH enzyme activity.

Clin. Chim. Acta 188, 49-58 (1990). TLC as auxiliary method for determination of the reaction product of an enzyme assay. TLC of galactose, galactose 1-phosphate, N-acetylglucosamine, N-acetyllactosamin, UMP, UDP, and UDP-galactose on silica with (1) isopropanol - MEK - ethyl acetate - butanol - water 6:5:3:2:5 and (2) ethyl acetate - pyridine - water 6:3:1. For solvent (2) the plate was impregnated with 0.2 M Na2HPO4 buffer. Three detection methods: UV fluorescence, spraying with sulfuric acid - acetone 1:10 and counting of the radioactivity of 3H-marked substances on the plate. Discussion of the influence of manganese in the medium on doubling of the UDP-galctose peaks.

Anal. Biochem. 308 (1), 106-111 (2002). TLC of cyclic AMP (cAMP) on silica gel with water - ethanol - NH4HCO3 3:7:0.2 M. This procedure separated [32P]cAMP from other radioactive metabolites of [32P]ATP in up to 19 samples on one sheet (20×10 cm) over 40–60 min at room temperature (21 °C). This simple and rapid isolation method provides a novel and convenient technique for the assay of adenylyl cyclase.

PLoS ONE 8(3), e57908 (2013). Feline SD (Sandhoff disease) fibroblasts GM2 SV3 and human TSD (Tay-Sachs disease) glial cells were transfected to express hybrid subunits H1 and H2 of beta-hexosaminidase A (Hex) and grown for 18 h in medium containing 4.7 µg/mL NBD-GM2 (2-nitro1,3-benzoxadiazol fluorescent derivative of GM2 ganglioside, substrate of Hex) and 50 µM CBE (conduritol-B-epoxide). To check the transfection, HPTLC of glycosphingolipids, extracted according to Folch’s method into acidic and neutral glycolipids, on silica gel first with chloroform – acetone 1:1, followed by chloroform – methanol – 0.2% CaCl2 55:45:10; the separated gangliosides (NBD-GM2 and its breakdown NBD-products) were quantified by a fluor image analyzer (Storm Imager). Total ganglioside fractions obtained through ion-exchange chromatography from transfected SD lysates were incubated with NBD-GM2 and separated on HPTLC, with the same first mobile phase followed by chloroform – methanol – water 65:25:4; the reaction product NBD-GM3 appeared only when GM2 activator protein was added during the incubation.

J. Planar Chromatogr. 3, 90-91 (1990). In situ measurement of the reaction mixture (1 mmol/L L-TAPA in 50 mmol/L Tris-HCL-buffer, pH 8.2, containing 25 mmol/L calcium chloride) and 0.1 mL of a trypsin containing sample on cellulose by absorbance at 405 nm. Sample size: 1 µL. - Densitometer response was linear in the concentration range from 10 to 200 µg of trypsin per mL; very good agreement between standard procedure and the microassay, good reproducibility.

Biochem. Biophys. Res. Commun. 470, 168-174 (2016). HPTLC of glycosphingolipid during the evaluation of enzyme activities of human Gb3/CD77 synthase supplemented with UDP-[14C]Gal on silica gel with chloroform – methanol – water 11:9:2. Detection of radiolabeled reaction products by exposure to phosphor screens for 8 weeks in -80 °C, followed by scanning. In parallel staining was used to facilitate identification of bands on the phosphor screens by spraying the plates with orcinol (0.2 %) in 3 M aqueous sulfuric acid, followed by heating at 110 °C for 10 min.

Anal. Biochem. 200, 27-30 (1992). TLC of the substrate from products of [14C] bilirubin formation in a coupled enzyme as involving hemo oxygenase and biliverdin reductase actions. Quantification by liquid scintillation counting of radioactive material on chromatograms. Also autoradiography.