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.
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.
Anal. Biochem. 286, 297-300 (2000). 1-ml aliquots of reaction mixtures were quenched by loading directly on silica gel TLC plates. Separation of residual glucose-1-phosphate from polymeric glucans with n-butanol - isopropanol - acetic acid - water 3:12:4:4. Visualization by spraying or dipping with acetic acid - H2SO4 - anisaldehyde 100:2:1.
J. of Chromatogr. A 1218 (20), 3089-3084 (2011). Comparison of the separation of the structurally related angiotensin-converting enzyme (ACE) inhibitors lisinopril, cilazapril, ramipril and quinapril and their corresponding active diacid forms (prilates) by conventional TLC on silica gel with the separation on monolithic ultra-TLC (UTLC) phase. Technical modifications of the commercially available equipment for sample application, development and detection were necessary for the use with UTLC plates. Development in a modified horizontal developing chamber with ethyl acetate - acetone - acetic acid - water 16:4:1:2. Detection by absorbance measurement at 220 nm and after exposure to iodine vapors under daylight, as well as by image analysis. As a result the monolithic layer was more efficient for the separation of structurally similar polar compounds, such as prilates, than conventional silica layers. Confirmation of the identity of the compounds by ESI-MS after their online extraction from the UTLC and TLC plates.