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:

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      130 141
      Two-dimensional high-performance thin-layer chromatography for the characterization of milk peptide properties and a prediction of the retention behavior – a proof-of-principle study
      M. TREBLIN, T. VON OESEN, L.-C. CLASS, G. KUHNEN, I. CLAWIN-RÄDECKER, D. MARTIN, J. FRITSCHE, S. ROHN* (*Department of Food Chemistry and Analysis, Institute of Food Technology and Food Chemistry, Technical University of Berlin, Berlin, Germany; rohn@tu-berlin.de)

      J Chromatogr A 1653, 462442 (2021). Samples were peptides obtained through tryptic hydrolysis of the 5 most abundant milk proteins: α-lactalbumin (α-LA), β-lactoglobulin (β-LG), α-, β- and κ-casein (CA). As standards, synthetic whey and pea (Pisum sativum, Fabaceae) peptides (selected based on the in silico tryptic digest of α-LA, β-LG, legumin A, and vicilin with one or zero miscleavages) were only used in the last assay for prediction of the RF values of peptides with known amino-acid (AA) sequences. Two-dimensional HPTLC on silica gel (pre-washed with methanol and activated 10 min at 100°), first with basic mobile phase sec-butanol – pyridine – ammonia – water 39:34:10:26, and (after 12h drying) in the orthogonal direction with acidic mobile phase sec-butanol – pyridine – acetic acid – water 11:8:2:5. Derivatization for peptides and proteins by immersion into fluorescamine (0.05 % in acetone); visualization under UV 254 nm and 365 nm. Computer-assisted determination of the x- and y-coordinates of the derivatized zones. Repeatability (n=8) of the 2D-HPTLC was statistically tested with the Kolmogorov-Smirnov test for normal distribution and with Dixon’s Q test for outliers. Relative standard deviation (RSD) for the RF values was 12.9 % for the first dimension (y-coordinates) and 16.5 % for the second dimension (x-coordinates). According to their higher intensity and sharpness, 15 – 20 detected zones from each protein hydrolyzate were selected, manually scraped from the derivatized layer, dissolved in formic acid solution (0.1 % in acetonitrile – water 3:2), mixed with an equal volume of matrix (dihydroxybenzoic acid 2 % in acetonitrile – water 3:7), crystallized on air on a ground steel target, before being desorbed by the laser beam of the MALDI-TOF-MS/MS (matrix-assisted laser desorption/ionization time-of-flight tandem mass spectrometry). Direct hyphenation of HPTLC to MS was not performed, to avoid zone diffusion during plate coating with the matrix and to circumvent the stronger binding of polar peptides on the layer.  The MS spectra were acquired in positive reflector mode in m/z range 340 – 4000 (10 – 2500 for fragments), using an external peptide as calibration standard. Identification of 51 from the 85 selected peptides according to AA sequences was performed, using software programs allowing m/z calculation of protein fragments and estimation of cleavage sites. Correlation of the retention behaviour of the peptides with their properties (molecular weight MW, isoelectric point IEP, charges, polarity) was tested with Student’s two-sided t-test after calculation of Pearson’s correlation coefficients. The correlation was significant with IEP, percentages of anionic AA and of non-polar AA; but not with the following properties: MW, percentages of cationic AA and of uncharged polar AA. Finally, based on the correlation results, regression formulas were found to calculate the x- and y-coordinates of any known peptide from the percentage of non-polar AA (or vice-versa). The prediction power of these formulas was verified by repeating the complete 2D-HPTLC-MS experiment with the standard peptides of whey and of peas, and measuring the absolute and relative deviations between the actual x- and y-coordinates and the predicted values. The absolute deviations were higher in the lower RF zones. The average, relative RF value deviations (range 22.1 – 25.7 %) were not different between whey and pea peptides.

      Classification: 2c, 2d, 4e, 18b, 19, 32e
      114 045
      Possibilities and limitations in the analysis of covalent interactions between phenolic compounds and proteins
      S. ROHN* (*Institute of Food Chemistry, Hamburg School of Food Science, University of Hamburg, Grindelallee 117, 20146 Hamburg, Germany, rohn@chemie.uni-hamburg.de)

      Food Res. Int. 65, 13-19 (2014). Review of the challenges and limitations in the analysis of polyphenol-protein interactions. The author described some properties of the HPTLC, such as the level of resolution that can be obtained with 2D-HPTLC and the coupling with mass spectrometry, that make this tool a promising alternative for the analysis of protein-phenol adducts.

      Classification: 1, 7, 19
      75 195
      Analysis of immunoglobulins by two-dimensional gel electrophoresis
      J.-D. TISSOT*, F. SPERTINI, (*Fondation Cent. de Transfusion de la Croix-Rouge, Suisse, Rue du Bugon 27, CH-1005 Lausanne, Switzerland)

      J. Chromatogr. 698, 225-250 (1995). A review with 237 references on the indications and limitations of high-resolution two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) as an aid in the analysis of the clonality of immunoglobulins with regard to „standard“ techniques such as immunofixation electrophoresis. Discussion of the use of the technique in laboratories experienced in defining monoclonal gammopathy both for diagnostic and for research purposes.

      Keywords: review
      Classification: 19, 36
      78 029
      Applications of SYPRO Orange and SYPRO Red protein gel stains
      TH.H. STEINBERG, L.J. JONES, R.P. HAUGHLAND, V.L. SINGER*, (Mol. Probes, Inc., Eugene, Oregon 97402, USA)

      Anal. Biochem. 239, 238-245 (1996). Characterization of the sensitivity and specificity of SYPRO Orange protein gel stain and SYPRO Red protein gel stain with native and 2-dimensional polyacrylamide gels and for staining gels prior to Western blot analysis. Comparison with commonly used staining techniques. Demonstration of the application of the stains in monitoring protein induction in bacterial overproducing strains. Presentation of protocols to detect proteins with these dyes in native gels. Discussion of the effect of staining proteins in transfer buffer prior to Western blotting on the sensitivity of subsequent immunodetection.

      Keywords:
      Classification: 3e, 19, 36
      88 193
      Characterization of clotting factor IX in plasma-derived preparations by electrophoretic techniques
      K. POCK*, A. BUCHACHER, A. RIZZI, D. JOSIC (*Octapharma Pharm. Produk. mbH Oberlaar Str. 235, 1100 Vienna, Austria)

      J. Chromatogr. A, 921 (1), 57-67 (2001). Characterization of clotting factor IX preparations from human plasma (pdFIX) using electrophoretic methods like SDS-PAGE, isoelectric focusing and 2-D PAGE. Separation of factor IX prior to and after activation with factor XIa by 1-D and 2-D PAGE and on isoelectric focusing gels. Identification of vitronectin by immunological techniques as major accompanying plasma protein, separated from Factor IX and characterized by isoelectric focusing and 2D-PAGE.

      Keywords:
      Classification: 19, 36
      115 015
      Application of thin-layer chromatography, X-ray fluorescence spectrometry, and Fourier transformed infrared spectroscopy in the analysis of binding media present on mummies of St
      Iva REZIC*, D. MUDRONJA, M. OBRANOVIC, T. REZIC, Ksenija SKARIC (*Faculty of Textile Technology, University of Zagreb, Croatia, iva_rezic@tff.hr)

      Giovanni Olini (1200 AD) and St. Nicolosa Bursa (1500 AD). J. Planar Chromatogr. 28, 205-212 (2015). TLC of (1) proteins, (2) resins, (3) sugars, and (4) waxes from fragments of the surface-coating material found on mummified bodies on silica gel for (2), (3), and (4), and on cellulose phase for (1) with n-butanol - acetic acid - water 4:1:1 for (1), benzene - methanol 19:1 for (2), acetonitrile - water 17:3 for (3), and petroleum ether - diethyl ether - acetic acid 90:10:1 for (4). Detection was performed after derivatization with ninhydrine reagent for (1), and iodine reagent for (2), (3) and (4). The combination of TLC and other chemical methods proved to be an effective and low-cost tool for obtaining valuable information during the archaeological investigation.

      Classification: 4e, 10, 11, 19
      76 095
      Polyacrylamide gel electrophoretic methods in the separation of structural muscle proteins
      K. BARANY*, M. BARANY, C.S. GIOMETTI, (*Dept. Physiol. & Biophys., Mail Code 901, Coll. Med., Univ. Illinois at Chicago, 901 South Wolcon Avenue, Chicago, IL 60612-7342, USA)

      J. Chromatogr. 698, 301-332 (1995). A review with 179 references on one- and two-dimensional gel electrophoretic methods for qualitative and quantitative investigation of the muscle proteins, with emphasis on the determination of protein phosphorylation. Demonstration of protein alterations in human neuromuscular diseases by two-dimensional gel electrophoresis.

      Keywords: review
      Classification: 19, 36
      78 078
      Mobile phase effect on membrane protein elution during immobilized artificial membrane chromatography
      CH. PIDGEON*, SONG JUN CAI, C. BERNAL, (*Dept. Med. Chem., Sch. Pharm., Purdue Univ., West Lafayette, IN 47907, USA)

      J. Chromatogr. A 721, 213-230 (1996). Study of different mobile phases for eluting membrane proteins from immobilized artificial membrane (IAM) chromatography surfaces using two protein mixtures containing bovine pancreatic PLAz. SDS-PAGE of the protein mixtures. Evaluation of the methods for their ability to selectively purify PLAz. Discussion of the elution conditions. Purification of PLAz from the two mixtures to electrophoretic homogeneity with 417- and 660-fold increase in specific activity in one step, based on silver-stained electrophoretic protein gels.

      Keywords:
      Classification: 19, 36