scholarly journals Impact of Hydrogen Ion Concentration on Amino Acids Composition of Macadamia Protein: Approached Using Cation-Exchange Chromatography

2016 ◽  
Vol 04 (10) ◽  
pp. 6-14
Author(s):  
Jianzhi Ye ◽  
Zhiping Han ◽  
Wei Tan
Nature ◽  
1945 ◽  
Vol 155 (3924) ◽  
pp. 49-49
Author(s):  
J. N. MUKHERJEE ◽  
S. K. MUKHERJEE

1963 ◽  
Vol 16 (3) ◽  
pp. 411 ◽  
Author(s):  
D Ilse ◽  
P Edman

In an attempt to extend the application of the phenylisothiocyanate degradation of peptides it was found necessary to study the kinetics of the conversion of phenylthiocarbamyl amino acids into phenylthiohydantoins. The conversion was found to obey first-order kinetics and to be catalyzed by hydrogen ions. A set of conditions with regard to time, hydrogen ion concentration and temperature was found, which allowed the quantitative or near quantitative conversion of all phenylthiocarbamyl amino acids into phenylthiohydantoins with the only exception of the phenylthiohydantoin of serine, which was returned in a yield of 20%.


1969 ◽  
Vol 22 (6) ◽  
pp. 1455 ◽  
Author(s):  
BA Moss ◽  
EOP Thompson

The haemoglobins of the adult domestic fowl were resolved by cation-exchange chromatography into two distinct components (designated Hb I and Hb II) in a ratio about 3 : 1. A third minor acidic component, Hb III, representing only 1 % of the total was also present. Hb I and Hb II and each of their globin subunits (0:1, pI; o:II, PII) were subjected to amino acid analysis. As reported by other workers, Hb II was found to have more of the dicarboxylic amino acids and less of the dibasic amino acids than Hb 1.


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