By Andreas Manz, Petra S Dittrich, Nicole Pamme, Dimitri Iossifidis
Interdisciplinary wisdom is changing into increasingly more vital to the fashionable scientist. This textbook covers bioanalytical chemistry (mainly the research of proteins and DNA) and explains every little thing for the nonbiologist. Electrophoresis, mass spectrometry, biosensors, bioassays, DNA and protein sequencing aren't often integrated in traditional analytical chemistry textbooks. The booklet describes the elemental ideas and the functions of instrumental and molecular equipment. it's really necessary to chemistry and engineering scholars who have already got a few wisdom approximately analytical chemistry.
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Extra resources for Bioanalytical Chemistry
3 Afﬁnity Chromatography Afﬁnity chromatography makes use of the highly speciﬁc molecular recognition of certain biomolecules. By attaching a speciﬁc ligand such as an antigen to the stationary phase material, the matching antibody can be speciﬁcally and reversibly adsorbed. Molecular recognition does not only occur between antigens and antibodies. Other bonding partners exist, including enzyme and co-enzyme, receptor protein and hormone or single strands of oligonucleotides and their matching counterparts.
H. Freeman, 2000. This page intentionally left blank Chapter 2 CHROMATOGRAPHY In this chapter, you will learn about . . ♦ . . the principles of separation in chromatography. ♦ . . the basic separation theory. ♦ . . chromatographic methods which are commonly applied to the separation of biomolecules. Chromatography is used routinely in almost every (bio)chemical laboratory for a large number of tasks. These range from the separation of mixtures on an analytical as well as preparative scale, from puriﬁcation and preconcentration of an analyte, to controlling the progress of a chemical reaction.
Fig. 12. Large molecules are un-retained and eluted ﬁrst, smaller molecules are retarded by the pores of the stationary phase. The chromatographic column is ﬁlled with a porous material such as a polymeric gel or agarose beads with diameters of typically 10 to 40 µm. Separation occurs, if the pore size is comparable to the size of the molecules passing through them (Figs. 12). Large molecules cannot enter the pores. They pass the matrix unretained and elute together with the solvent front. Smaller molecules enter the pores and have an average residence time, which depends on the size and shape of the molecule.