J. Planar Chromatogr. 9, 35-38 (1996). TLC of tryptophan on silica with 2-propanol - NH3 (25%) 7:3. Detection of amino acids by dipping into a solution of 0.3% ninhydrin in acetone - acetic acid 97:3. Detection of tryptophan by spraying or dipping with/into 4-(dimethylamino)benzaldehyde solution. Quantification by densitometry at 625 or 276 nm.

J. Agric. Food Chem. 45, 189-194 (1997). TLC of glutamic acid, asparagine, aspartic acid, pyroglutamic acid, gamma-glucBCA, BCA on cellulose with 1-butanol - pyridine - acetic acid - water 15:10:3:12. Detection by spraying with 0.1% ninhydrin in acetone and/or a modified Reindel-Hoppe reagent: exposure to chlorine vapor for 10 min, aeration, followed by spraying with 0.1% 3,3',5,5'-tetramethylbenzidine (in place of the carcinogenic o-toluidine) in ethanol.

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. Liq. Chrom. & Rel. Technol. 25, 2345-2349 (2002). HPTLC of 19 amino acids (i. a. histidine, lysine, alanine, methionine, threonine, asparagine, proline, and leucine/isoleucine) on i.a. silica gel with preadsorbent sample application zone and on cellulose with n-butanol - acetic acid - water 3:1:1. Detection of the zones was achieved by spraying the developed and air-dried plates with ninhydrin reagent, air drying for 30 min and heating for 10 min at 110°C. Densitometry at 495 nm for histidine and 610 nm for all other acids.

J. Liq. Chromatogr. Relat. Technol. 28, 2261-2271 (2005). HPTLC of 21 butylthiocarbamyl-amino acids on silica gel in a saturated horizontal chamber. Pre-chromatographic derivatization with 2-propanol - BITC - triethylamine was carried out after application of the amino acids. For the reaction the plate was placed in a glass chamber in a thermostat at 40 °C for 30 min. Then the plate was developed with ethanol - methanol - chloroform 1:1:2. Detection by spraying with a freshly prepared mixture of 3 % sodium azide and 0.5 % starch solution adjusted to pH 5.5 and exposed to iodine vapor for 5 s. Quantities in the range of 2-90 pmol per spot were detected.

J. Chromatogr. A 1526, 157-166 (2017). Introduction of a promising alternative method for protein analysis using HPTLC with its high level of variability regarding the chromatographic system (multiple mobile and stationary phases, even mixed) and manifold detection as well as hyphenation possibilities. Silica gel, cellulose, and different RP layers were investigated with regard to their applicability for HPTLC-immunostaining. HPTLC of intact proteins on silica gel with 2-butanol – pyridine – ammonia – water 39:20:10:31; on cellulose with 2-butanol – pyridine – ammonia – water 32:30:11:25; and on RP phase with acetonitrile – trifluoroacetic acid – water 400:30:37. After development the plate was incubated with Tween20 as blocking reagent in a small vessel to inhibit unspecific binding of the antibodies to the surface. Then the plate was incubated for 2 h with the primary antibody solution and after washing with the secondary antibody for 1 h. Detection by incubating the plate in a dying solution containing 0.06% 3,3',5,5'-tetramethylbenzidine, 0.2% dioctyl sulfosuccinate sodium salt, 0.7% citric acid monohydrate, 1.8% sodium hydrogen phosphate dihydrate, 25% ethanol, and 1.5‰ dihydrogen dioxide, until blue zones appeared under white light. For the example analysis of beta-lactoglobulin on silica gel using antibovine beta-lactoglobulin antibodies, linearity was in the range of 75-2000 ng, the LOD was 62 ng/zone, the LOQ 93 ng/zone, and the accuracy 98.3%.

Anal. Biochem. 157, 19-27 (1986). Description of a two-dimensional mapping procedure, involving electrophoresis in the 1st direction and TLC in the 2nd direction. Glycopeptide maps produced for the model proteins alpha, -acid glycoprotein and fetuin, as well as for the two surface glycoproteins gp9O and gp45 from equine infectious anemia virus.

J. of Medicinal Chemistry 32, 244-247 (1989). TLC of peptides on silica with butan-1-ol - acetic acid - water 4:1:5 (upper phase), chloroform - methanol 7:3, butan-1-ol - acetic acid - water - pyridine 15:3:3:10 and butan-1-ol - acetic acid - water 4:1:1. Detection by exposing to iodine vapor.