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.
Chromatogr. (Se Pu) 3, 194-198 (1985). (Chinese) (The thin-layer electrophoresis behaviours of 33 metal ions on the stannic arsenate layer.) Study of the thin-layer electrophoresis behaviours of 33 metal ions on stannic arsenate layer with 0.1 M tartaric acid, 0.1 M citric acid and 0.01 M hydrochloric acid. Investigation of TLE parameters.
J. Chromatogr. 698, 351-359 (1995). Test of transfer efficiency from polyacrylamide gels and binding to Immobilon P and CD in different buffers with 125I-labelled proteins. Staining of Immobilon CD with toluidine blue and iodine vapor. Comparison of staining protocol on Immobilon CD. Discussion of structural analysis on blotted and stained proteins, and of the transfer conditions.
J. Chromatogr. A 773, 299-309 (1997). Protein purification by using a combination of molecular mass exclusion membranes with electrophoresis. Description of the method for fractionation of proteins from complex protein mixtures by reflux electrophoresis using the Gradiflow, which allows rapid method development for defining optimal conditions and shortening times, resulting in higher yields.
IX. Dünnschitelektrophoretische Trennung der polysaccharidhaltigen Dickungsmittel. (Thin-layer electrophoretic separation of polysaccharide - containing thickeners.) Z. Lebensm. Unters. Forsch. 181, 40-44 (1985). TLC separation of polysaccharides on silanized silica in sodium borate buffer 0.3 mol/l, pH 10. Separation of neutral and acidic polysaccharides with acetic acid - sodium acetate buffer 0.1 mol/l, pH 6.
J. Chromatogr. 698, 341-349 (1995). Two-dimensional gel electrophoresis in polyacrylamide for mapping the proteins in lysates of the arcaeon P. furiosus and in analyzing enzymes purified from P. furiosus. Determination of the location of the enzymes in the 2DE maps by comigration of lysate proteins with purified enzymes. Production of a 2DE map of furiosus proteins with some identification. Investigation of the usefulness of 2DE for the evaluation of the purity of enzyme preparations and for the characterization of their subunit structure under denaturing conditions.
SYPRO Orange and SYPRO Red protein gel stains on-step fluorescent staining of denaturing gels for detection of nanogram levels of protein. 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. B 692, 303-310 (1997). Separation by acetic acid - urea - PAGE according to the charge, and then by SDS-PAGE according to molecular mass. Detection by Immuno-precipitation and Westen blots of the peptides.