Cumulative CAMAG Bibliography Service CCBS

Our CCBS database includes more than 11,000 abstracts of publications. Perform your own detailed search of TLC/HPTLC literature and find relevant information.

The Cumulative CAMAG Bibliography Service CCBS contains all abstracts of CBS issues beginning with CBS 51. The database is updated after the publication of every other CBS edition. Currently the Cumulative CAMAG Bibliography Service includes more than 11'000 abstracts of publications between 1983 and today. With the online version you can perform your own detailed TLC/HPTLC literature search:

  • Full text search: Enter a keyword, e.g. an author's name, a substance, a technique, a reagent or a term and see all related publications
  • Browse and search by CBS classification: Select one of the 38 CBS classification categories where you want to search by a keyword
  • Keyword register: select an initial character and browse associated keywords
  • Search by CBS edition: Select a CBS edition and find all related publications

Registered users can create a tailor made PDF of selected articles throughout CCBS search – simply use the cart icon on the right hand of each abstract to create your individual selection of abstracts. The saved items can be printed to PDF using the print function of your web browser.

      126 063
      The interaction methylene blue and glutathione-S-transferase purified from human erythrocytes
      S. UZAN, H. ACAY, M. FIRAT, A. BILDEN, H. AYGUN* (*Department of Biology, Faculty of Science, Dicle University, 21280 Diyarbakir, Turkey, byaygun@gmail.com)

      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.

      Classification: 20, 30a
      125 010
      Thin-layer chromatography-bioautographic method for the detection of arginase inhibitors
      R. ATTIA, A. ZEDET, M. BOURJOT, E. SKHIRI, C. MESSAOUD, Corine GIRARD* (*PEPITE EA4267, University of Bourgogne Franche-Comté, 19 rue Ambroise Paré 25000 Besançon, France, corine.girard@univ-fcomte.fr)

      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.

      Classification: 20
      124 004
      Detection and identification of acetylcholinesterase inhibitors in Annona cherimola Mill. by effect-directed analysis using thin-layer chromatography-bioassay-mass spectrometry
      O. GALARCE, J. PAVON, K. HENRIQUEZ, M. ARANDA* (*Laboratory of Advanced Research on Foods and Drugs, Department of Food Science and Technology, Faculty of Pharmacy, University of Concepcion, Barrio Universitario s/n Concepción, Chile, maranda@udec.cl; maranda@gmx.net)

      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.

      Classification: 20
      102 064
      Characterization of a novel debranching enzyme from Nostoc punctiforme possessing a high specificity for long branched chains
      J. CHOI (Choi JiHye), H. LEE, Y. KIM (Kim Youngwan), J. PARK (Park Jongtae), E. WOO (Woo Euijeon), M. KIM (Kim Myojeong), B. LEE (Lee Byonghoon), K. PARK (Park Kwanhwa)* (*Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, Seoul National University, Seoul, Republic of Korea, parkkh@snu.ac.kr)

      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.

      Classification: 20
      58 052
      Separation of (1-3H) cellooligosaccharides by thin-layer chromatography
      W.J. CHIRICO, R.D. BROWN JR.

      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.

      Classification: 10a, 20
      85 016
      5-(pentaflourobenzoylamino)fluorescein - A selective substrate for the determination of glutathione concentration and glutathione S-Transferase activity
      S. ARTTAMANGKUL, M.H. MAHESH, R.P. HAUGLAND*, Z. DIWU, J. LIU, D. H. KLAUBERT, R. P. HAUGLAND, (*Molecular Probes, Inc., 4849 Pitchford Avenue, Eugene, Oregon, 97402-9165; RosariaHaugland@probes.com)

      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.

      Keywords:
      Classification: 3e, 18a, 20, 32
      104 020
      HPTLC and HPLC-MS quantification of coenzyme Q10 and cholesterol in fractionated chicken-breast tissue
      Petra JAZBEC*, A. SMIDOVNIK, M. PUKLAVEC, M. KRIZMAN, J. SRIBAR, L. MILIVOJEVIC, M. PROSEK (*Department of Food Chemistry, National Intitute of Chemistry, Ljubljana, Slovenia; Petra.jazbec@ki.si)

      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.

      Classification: 9, 20
      60 119
      Rapid and sensitive thin-layer chromatographic assay procedure for measuring xanthine dehydrogenase activity from tissue extracts
      S. K. FROST*, M. E. BORCHERT, S. THORSTEINSDOTTIR, (*DSP. Physiol. & Cell Biol., Univ. Kansas, Lawrence, KS 66045, USA)

      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.

      Classification: 20