Peptides electrophoretic purification

Fig. 14.6 Microreactor manifold for synthesis and electrophoretic purification of peptides.

The isoelectric point of the peptide isolated from cow is pH 8.5. This property is a basis for a method of electrophoretic purification (309). 

For rapid confirmation of the molecular mass of a recovered peptide following RPC purification, either ESI-MS or MALDI-MS procedures are now indispensable. Studies on the interaction of peptides with solvent molecules, ions, and free or immobilized ligands in chromatographic or electrophoretic environments have, however, been largely confined to methods that examine global properties of different peptides in the bulk mobile phase. In... 

An early attempt to produce a recombinant human 29-amino acid antimicrobial peptide SMAP29 in tobacco was reported by Morassutti et al. (2002) who used a chitin-binding domain for purification and an associated intein cleavage system to release the peptide. Expression levels appeared to be low, with the peptide associated with plant proteins. Upon electrophoretic separation, the peptide displayed the expected immunological and biological activites. 

Electrophoretic techniques, such as two-dimensional electrophoresis or isoelectric focusing, lend themselves under appropriate conditions to the separation with excellent resolution of small amounts of samples. They have mainly found use as powerful methods of analysis since their general applicability in the areas of peptide purification and isolation has, until recently, been severely restricted by limitations in sample capacity and instrumental design. 

Thymomodulin. Leucotrofina. Cell-tree thymic hormone preparation extracted from calf thymus by acid hydrolysis Composed of a mixture of biologically active acidic peptides of mol wt < 10,000. Modulates the maturation of T-cells, Prepn of crude extract from calf thymus B, Bruneiti, E. Pini, US. pat. 3,657,417 (1972 to Eltem). Electrophoretic characterization C. Secchi er at.. Rip. Ear. Set. Med. Farmacol. 4, 499 (]982), C.A. 01, 21878m (]9S4). Biological activity and comparison with other thymic hormones J. J. Twomey, N, M, Kouttab. Cell. Immunol 12, 186 (1982). Purification and pharmacodynamics eidem. 

The relation between oxidation of monophenols and polyphenols has been investigated extensively by Nelson and his students. The nature of the reactions studied is still not clear, but many interesting aspects have been explored. As in the case of other workers, it was found that there is a tendency for the ability to oxidize monophenols (cresolase) to be lost on purification, while polyphenol oxidation (catecholase) is more stable. The ratio of catecholase to cresolase activity of purified preparations appears to vary with electrophoretic mobility, and it has been suggested that a peptide component is lost from the enzyme, and that the purified preparations represent partially degraded enzyme. ... 

The enzyme is widely distributed in animal tissues and microorganisms and has been purified by classical methods from several sources. - Multiple forms, which differ for electrophoretic mobility and molecular weight, have been observed in animal tissues in some cases the origin of these forms is due to the binding of catalytically inactive peptides or proteins to adenosine deaminase molecules. Recently, we have prepared a specific adsorbent, 9-(p-aminobenzyl) adenine bound to Sepharose, which allows the rapid and quantitative purification of the enzyme from several sources independently from the physicochemical properties of the multiple forms. ... 

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