J. Planar Chromatogr. 33, 263-269 (2020). HPTLC of the interaction between methylene blue and purified glutathione-S-transferase (5 mmol/L methylene blue and enzyme solution in 0.1 mol/L potassium phosphate buffer) on silica gel with butanol - acetic acid - water 12:3:5 for 2 h. Detection by spraying with ninhydrin (0.25 % in acetone). The complex that most likely came from the interaction of methylene blue and purified glutathione-S-transferase had a hRf of 16.

J. Sep. Sci. 43, 2477-2486 (2020). HPTLC of urea produced by arginase as a bioautographic method for the detection of arginase inhibitors in Myrtus communis on silica gel with ethyl acetate - methanol - water - formic acid 800:100:100:1. Detection by spraying with arginase solution (50 U in 3 mL of a buffer containing Tris–HCl 50 mM, pH 7.5 and 0.1 % of BSA), followed by spraying with 3 mL of L-arginine solution (200 mM, pH 9.7) and incubation at 37 ºC for 60 min. Visualization by spraying with 3 mL of sulfuric acid - phosphoric acid - water 2:7:91 and 2 mL of alpha-isonitrosopropiophenone solution (5% in absolute ethanol) followed by heating at 100 ºC for 1h. The hRF value for the inhibitor N-trans-caffeoyltyramine was 27. Sensitiviy was estimated for the arginase inhibitor Nω-hydroxy-nor-Arginine (nor-NOHA), resulting in a LOD of 0.1 µg/zone.

Phytochem. Anal. 30, 679-686(2019). HPTLC-Acetylcholinesterase bioassay of cherimoya fruits on silica gel with the enzyme substrate 1‐naphthyl acetate (1.5 mg/mL). Enzymatic solution was sprayed (1 U/mL in 50 mM Tris–HCl buffers at pH 7.8), followed by incubation at 37 ºC for 10 min. A Fast Blue B salt aqueous solution (1.0 mg/mL), freshly prepared, was sprayed onto the plate to obtain a purple background. Further analysis by HPTLC-MS allowed the characterization of three potential AChE inhibitors: anonaine, glaucine and xylopine.

Biochem. Biophys. Res. Commun. 378, 224-229 (2009). TLC of the hydrolytic action patterns of the purified Nostoc punctiforme debranching enzyme on the following substrates: pullulan, amylopectin, soluble starch, amylose, cyclodextrins, and maltooligosaccharides (form glucose to maltoheptaose), on silica gel with 1-propyl alcohol – ethyl acetate – water 6:2:3. Detection by dipping into 0.3 % N-(1-naphthyl)-ethylenediamine and 5 % sulfuric acid in methanol, followed by heating for 10 min at 110 °C. Quantitative determination by radioactivity measurement of the 14C-labeled maltooligosaccharides.

assay for cellulolytic enzymes. Anal. Biochem. 150, 264-272 (1985). TLC of the title compound on silica with ethyl acetate - water - methanol 8:3:4. The method facilitates analysis of the activity of cellulolytic enzymes. Also separation of cellooligosaccharides using other adsorbents, solvents and impregnants.

Anal. Biochem. 269, 410-417 (1999). Quantitative analysis of glutathione (GSH) or of glutathione S-Transferase (GST) activity using a new fluorescent molecule, 5-(pentaflourobenzoylamino)fluorescein (PFB-F). TLC of the formed glutathione adduct, GS-TFB-F, and of excess PFB-F on silica gel 60F254 with 1-butanol - methanol - water 3:1:1. The GS-TFB-F adduct spots were quantified with a fluorescence plate scanner using the blue fluorescence/chemifluorescence (480 nm) mode. Detection limits for GSH and for GST activity were 10 pmol/(l and 1 ng/(l, respectively.

J. Planar Chromatogr. 22, 395-398 (2009). HPTLC of coenzyme Q10, cholesterol and biological extracts on silica gel with petroleum ether - diethyl ether - acetic acid 85:15:1. Detection by dipping into 5 % phosphomolybdic acid in ethanol for 10 s followed by heating for 10 min at 110 °C. Quantitative evaluation in visible light.

J. Chromatogr. 382, 314-320 (1986). TLC of xanthine dehydrogenase on silica - cellulose with propanol -7% NH3 2:1. Measurement by fluorodensitometry at 366 nm.