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Advances in protein chemistry Volume 2 by M. L.; Edsall, John T. (Eds) Anson

By M. L.; Edsall, John T. (Eds) Anson

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The highly insoluble copper salt is today in general use for the last stages of isolating aspartic acid (314). The different solubilities of the various pure aminoacid copper salts in water and alcohols led to the proposal of solvent extraction of dried copper salts as a method of separating the amino acids in protein hydrolyzates (340). This method of separation is theoretically unsound, owing to mixed complex formation and to the mixed crystallisation and mutual solubility effects already mentioned.

Such interference has been too little recognized in the literature, and many workers are unaware of the deleterious effects that such a common substance as alcohol exerts on the amino-N determination. The effect of light on the reaction of tyrosine in the determination has recently been discussed (428, 428a). , 429) and is likely to give place to direct determination of these amino acids. Olcott (430) has proposed to estimate glutamic acid by the decrease in amino-N due to pyrrolidone-carboxylic acid formation on autoclaving a protein hydrolyzate, and gives a bibliography of other attempts to determine glutamic acid by pyrrolidone-carboxylic acid formation.

SYNGE ing threonine. Winnick (474) has described a modification employing microdiffusion. The formaldehyde (from serine and/or hydroxylysine) remaining in the reaction mixture is determined by Nicolet and Shinn (475)by precipitation as its dimedone derivative. Boyd and Logan (476)distil out the formaldehyde and determine it by a specific colorimetric procedure. We (411) encountered difliculties in quantitative precipitation of formddehyde-dimedone from protein hydrolyzates, and Mr. M. W. Rees (private communication) informs us that this has been his experience also.

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