Amino Acids, Peptides and Proteins: An Introduction by H.D. Jakubke, J. Jeschkeit

By H.D. Jakubke, J. Jeschkeit

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The industrial preparation of methionine (40000 tons in 1972, major use as an additive for poultry food) is by the STRECKER synthesis from P-methylmercaptopropionaldehyde CH 3-S-CH 2CH 2-CHO, which is in turn obtained by the addition of methyl mercaptan to acrolein. Aspartic acid is obtained by a continuous process from maleic acid and ammonia. 1. p. 110 °C) or with 8 N sulphuric acid. This reaction needs between 12 and 17 hours, because of the stability of peptide bonds involving valine, leucine and isoleucine.

3. UV2 7 • 28 , JR 29 •30 and N MR Spectra 20- 24 •31 of Amino Acids While the aliphatic amino acids do not absorb in the. ultra-violet region above wavelengths of 220 nm, the aromatic amino acids tryptophan, tyrosine, phenylalanine and histidine show characteristic maxima above 250 nm. The high molar extinctions of tyrosine and tryptophan facilitate rapid quantitative determination of these amino acids in proteins. In the IR spectra of amino acids the normal NH-stretching frequencies in the region of 3300-3500 cm-1 are absent.

In this process electrophoresis and specific anion and cation exchange resins play an important role. Selective isolation of aromatic amino acids is possible by adsorption onto activated charcoal. Glutamic acid can be directly crystallised from a concentrated hydrolysate which has been saturated with hydrogen chloride. The separation methods which were used in the classical era of the subject, such as the fractional distillation of esters (E. FiscHER), the extraction of monoamino carboxylic acids with n-butylalcohol (H.

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