J. Planar Chromatogr. 26, 455-456 (2013). HPTLC of oligopeptides on RP-18 (chromatography described in R. Gwarda, A. Tomczyszyn, A. Misicka, T.H. Dzido, Acta Chromatogr., in print, 2015). Detection by spraying or dipping for 2 s with 2 % ninhydrin solution in 1) acetone - glacial acetic acid 25:1 or 2) acetone - methanol - glacial acetic acid 25:25:2, followed by heating at 80 ºC. Results showed that short dipping of the plate in ninhydrin solution resulted in a better detectability of peptides than spraying it with the same solution. Solution 2) with methanol made the ninhydrin reaction faster, and colored all zones in a distinct pink/red color, unfortunately one peptide (no. 1) showed poor color intensity.

Chinese J. Herb Med. (Zhongcaoyao) 25, 377-378 (1994). Disc gel electrophoresis of water-soluble proteins of bile cysts of bear, as well as pig, cow and sheep on acrylamide (7.5%). Detection by dipping into a 0.025% brilliant Blue R250 solution. Densitometry at 560 nm. Identification of bile-cyst of bear by comparison with standard.

J. Chromatogr. 698, 123-143 (1995). A review with 166 references on the utilization of combined protein-labelling and staining methodologies in gel electrophoresis including selected applications in polyacrylamide gels and solid membrane matrixes.

J. Chromatogr. B 756 (1/2), 95-103 (2001). Identification and molecular characterization of the major allergen of plum by SDS-PAGE and immunoblotting with the sera of 23 patterns. Purification of the identified major allergen by HPLC. Further characterization by periodic-Schiff stain, isoelectro-focusing and N-terminal amino acid sequencing. Showing that the major allergen of plum is a 9 kD lipid transfer protein, mot glycosylated, with a base character and highliy homologous to the major allergen of peach.

J. of Chromatogr. A 1281, 135-141 (2013). The use of detergents for the extraction, solubilization and purification of membrane proteins (MPs) is necessary due to their hydrophobic nature. Detergent quantification is essential to routine analysis because the concentration of amphiphiles is crucial in the crystallization process. HPTLC of detergents (in small quantities, bound to solubilized MPs) on silica gel with dichloromethane – methanol – acetic acid 80:19:1. The optimum HPTLC conditions were investigated using n-dodecyl-beta-D-maltoside (DDM), the most popular detergent for membrane protein crystallization. Quantification by fluorescence measurement at 366 nm using a Hg lamp. The calibration curve was linear in the range of 100-1600 ng of DDM in water and the limit of detection of was 50 ng/zone, which is the best LOD achieved to date for a routine detergent assay (not modified by the addition of NaCl, commonly used in protein buffers). In comparison with other techniques (colorimetry, GC, and FTIR) the HPTLC method has the advantage of no prior sample treatment for concentration or extraction, and no chemical labeling is required. In comparison with TLC, the HPTLC method is 100 times more sensitive. The HPTLC method is suitable for routine analysis, assay results are obtained within 3 hours and only few microliters of sample are needed.

J. Chromatogr. 698, 203-224 (1995). A review with 149 references on the use of two-dimensional electrophoresis (2DE) to study naturally occurring protein mutations and polymorphisms as well as the charcterization of induced protein mutations in prokaryotes and eukaryotes. with several examples. Discussion of the advantages and disadvantages of 2DE in the detection of protein mutations.

Anal. Biochem. 239, 223-237 (1996). Presentation of two new fluorescent dyes for detection of proteins in electrophoretic gels using one-step procedures, with the stained protein being excited by UV 300 nm, or at visible wavelengths, and the excitation maxima of 472 nm for the Orange stain and 547 nm for the Red stain. Discussion of the sensitivity by comparison with other staining techniques and their limitation.

J. Chromatogr. 13, 756 (1/2), 141-150 (2001). Presentation of an overview of methods combining basic procedures in glycochemistry with various applications of electrophoresis that allow investigating single allergens in crude extracts. Analysis of various allergen extracts, e.g. from tomato, grass pollen and bacteria.