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The hydrophobic amino acids are reasonable choices, except for the puzzling absences ofα-amino-n-butyric acid, norvaline and norleucine.
The SAR of the amino acid indicates that the carboxylic acid is required for inhibition and that L-histidine is the most favored amino acid.
The results show that aspartic acid, glutamic acid, isoleucine, leucine, and lysine are the major amino acid components.
Journal ArticleDOI
Michiel Lodder, Bixun Wang, Sidney M. Hecht 
01 Jul 2005-Methods
34 Citations
In addition, an aminated analogue of the pentenoyl protecting group, the unnatural amino acid allylglycine, can be employed as part of the peptide backbone to afford a protein cleavable by iodine.
The major amino acids were: glutamic acid, leucine, valine, phenylalanine, lysine and alanine which approximately accounted for 50% of the total free amino acid content, probably indicating the preferential cleavage of peptide bonds by the proteolytic agents in the cheese.
These data suggest that valine is the fifth-limiting amino acid and that either histidine or isoleucine is the sixth-limiting amino acid in an 11% CP diet.
The non-detection of this amino acid in the other samples analyzed suggests that there are amino acid-containing and amino acid-free MMs, with ˜14% of the MMs containing AIB.
Other amino acid residues, such as histidine, might be also affected.
For every amino acid studied herein, the current results indicate that a proton is bound to the alpha-amino nitrogen, except for lysine, in which the protonation site is the amino nitrogen in the side chain.
Iodine-123-4-amino-3-iodobenzylguanidine ([123I]AIBG), an analog of 123I metaiodobenzylguanidine ([123I]MIBG), has an advantage in having a more rapid and simple synthesis.

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