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
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      131 079
      Equivalency calculation of unknown enzyme inhibitors in situ the adsorbent of effect-directed autograms
      E. AZADNIYA, Gertrud MORLOCK* (*Institute of Nutritional Science, and Interdisciplinary Research Center, Justus Liebig University Giessen, Heinrich-Buff-Ring 26-32, 35392 Giessen, Germany,

      Anal. Methods. 11, 4939-4945 (2019). HPTLC of Peganum harmala seeds on silica gel with ethyl acetate - methanol - ammonia (25%) 85:11:4. Detection under UV light at 254 and 366 nm. Track pattern application by applying each reference compound solution (physostigmine: 0.1–1.5 ng/zone; rivastigmine tartrate and piperine: 200–2000 ng/zone). A new piezoelectric spraying workflow was applied for the HPTLC-enzyme assay: the plate was sprayed with the enzyme solution (6.6 units per mL AChE or 3.3 units per mL BChE), followed by incubation at 37 °C for 25 min and spraying with 0.5 mL substrate-chromogenic solution and drying. The enzyme inhibition densitograms of both assays were measured by inverse scan at 546 nm using a mercury lamp. Equivalency of the AChE/BChE inhibition was calculated for two quantitative modes: applied and developed. A higher accuracy was obtained via an appropriate co-developed reference inhibitor for the enzyme inhibition equivalency calculation. 

      Classification: 4e, 20
      129 051
      Optimized high‑performance thin‑layer chromatography‒ bioautography screening of Ecuadorian Chenopodium quinoa Willd. leaf extracts for inhibition of α‑amylase
      Veronica TACO*, C. PALMIERI, P. DUEZ, A. NACHTERGAEL (*Facultad de Ciencias Químicas (UCE), Universidad Central del Ecuador, Quito, Ecuador,

      J. Planar Chromatogr. 34, 561-567 (2021). HPTLC of Ecuadorian Chenopodium quinoa Willd. leaf extracts on silica gel with formic acid - water - methyl ethyl ketone - ethyl acetate 1:2:4:3. Detection by heating at 105 °C for 60 min, followed by a three step derivatization method: 1) spraying with a 3 mL solution of α-amylase (5 U/mL of α-amylase in ethanol 10 %), followed by incubation at 37 °C for 30 min, 2) a 2 mL solution of starch (1 % of starch in ethanol 10 %) was applied on the plate, followed by incubation at 37 °C for 10 min, and (3) detection using iodine vapors for 2 min (1 g of solid iodine). The method allowed rapid localizing of α-amylase inhibitory compounds in complex plant matrices.

      Classification: 20
      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,

      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,

      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,;

      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
      55 080

      J. Neurochem. 44, 411-420 (1985). The known procedure of peptide mapping after tryptic fragmentation is performed 2-dimensionally by TLC on silica with propanol -34 % NH3 7:3, followed by TLE at pH 3.5, 800 V, 50 minutes with acetic acid - pyridine - water 10:1:300. The peptides are sprayed with fluorescamine, followed by triethylamine treatment, then visualized by UV.

      Classification: 20
      79 235
      Purification and assay methods for angiotensin-converting enzyme
      Q.CH. MENG*, S. OPARI, (*Vascular Biol. & Hypertension Program, Div. Cardiovascular Disease, Univ. Alabama at Birmingham, Birmingham, AL 35294-0007, USA)

      J. Chromatogr. A 743, 105-122 (1996). A review with 113 references on the historical development of ACE purifaction and assay methods, including SDS-PAGE with direct radioimmunoassay, or immune isolation with quantification by SDS-PAGE, and HPLC, etc.

      Classification: 20, 36
      56 095
      L-gulonolactone oxidase is present in the invertebrate, limulus polyphemus

      Experientia 41, 485-486 (1985). TLC of the 2, 4-dinitrophenylhydrazones of 1-gulonolacetone, l-ascorbic acid and other derivatives produced by enzymatic reaction on silica with ethyl acetate - chloroform - acetic acid - acetone 70:50:7:6. Comparison with authentic identification standards.

      Classification: 20