In AC Research: In AC Research

Oct 1, 2000 - scribe using fluorescence intensity correlation to enhance peak resolution and species identification in CE. To dem- onstrate the potent...
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in ac research

In AC Research contains brief introductions to the research articles appearing in the October 1 issue. A free updated table of contents is available on the Web (http://pubs.acs.org/ac).

Sequencing sulfated oligosaccharides from mucins Improving peak resolution in CE Lei Geng and Gufeng Wang at the University of Iowa describe using fluorescence intensity correlation to enhance peak resolution and species identification in CE. To demonstrate the potential of two-dimensional fluorescence correlation CE, the researchers simulate the base-calling step in four-color DNA sequencing using four fluorescent dyes with varying lifetimes. (“Two-Dimensional Fluorescence Correlation in Capillary Electrophoresis for Peak Resolution and Species Identification”; 10.1021/ac000534i; p 4531)

Separating yeast cells Richard D. Smith and colleagues at the Pacific Northwest National Laboratory describe the separation and identification of yeast cells at various stages of growth using capillary isoelectric focusing. The researchers report column efficiencies >4000 and suggest that the method might be generally applicable to separating cell populations based on phenotype or physiological state. (“Capillary Isoelectric Focusing of Yeast Cells”; 10.1021/ac000144w; p 4603)

Complexing viruses and antibodies Ernst Kenndler and colleagues at the University of Vienna (Austria) use affinity CE to investigate the formation of complexes of human rhinovirus with nonaggregating neutralizing monoclonal antibodies. At low antibody-to-virus ratios, peaks corresponding to the complexes are broad, indicating the presence of a heterogeneous population of virions with varying amounts of bound antibodies; at high ratios, the peaks are narrow, indicating saturation. (“Affinity Capillary Electrophoresis for the Assessment of Complex Formation between Viruses and Monoclonal Antibodies”; 10.1021/ac000250y; p 4634)

Gunnar C. Hansson and colleagues at Göteburg University (Sweden) use LC coupled to electrospray ionization MS/MS in the negative ion mode as part of a strategy for profiling diverse mixtures of sulfated mucin-derived oligosaccharides. From a single chromatographic analysis, the sequences of 28 sulfated mucin oligosaccharide alditols purified from porcine large intestine are elucidated, revealing prominent core sequences and terminal blood grouptype epitopes. (“Sequencing Sulfated Oligosaccharides from Mucins by Liquid Chromatography and Electrospray Ionization Tandem Mass Spectrometry”; 10.1021/ac000631b; p 4543)

specific binding of a second protein, the authors believe these substrates could be useful in label-free biomolecular assays. (“Orientations of Liquid Crystals on Mechanically Rubbed Films of Bovine Serum Albumin: A Possible Substrate for Biomolecular Assays Based on Liquid Crystals”; 10.1021/ac000256n; p 4646)

Cyclic AMP-recognizing oligopeptides Yoshiki Katayama and colleagues at Kyushu University, Mitsubishi Kagaku Institute for Life Sciences, and the Tokyo University of Pharmacy and Life Science (all in Japan) describe using the amino acid sequences of essential subsites in various cyclic AMP-dependent protein kinase families to design a 17-mer peptide ligand for cyclic AMP. (“Design of Cyclic AMP-Recognizing Oligopeptides and the Evaluation of Its Capability of Cyclic AMP Recognition Using Electrochemical System”; 10.1021/ac990847h; p 4671)

Sensor with protein-engineered enzymes Koji Sode and colleagues at the Tokyo University of Agriculture and Technology (Japan) describe an enzyme glucose sensor with an expanded dynamic range based on proteinengineered enzymes with a different Michaelis constant. The dynamic range is 0.5–30 mM with