Post-translational chemical modifications of proteins--III. Current developments in analytical procedures of identification and quantitation of post-translational chemically modified amino acid(s) and its derivatives.
1. The Chemical modifications of amino acids and their derivatives are mainly due to different post-translational enzymatic reactions. 2. The enzymatic reactions resulting in amino acids such as acetylation-, formylation, methylation-phosphorylation-, sulfation-, hydroxylation, ADP ribosylation-, carboxylation-, amidation-, adenylylation-, glycosylation-, ubiquitination-, prenylation and acylation are listed and analytical methods are reported and extensively reviewed. 3. The post-translationally modified cross-linking molecules after maturations such as desmosines, allo-desmosine, hydroxy-, lysylpyridinoline, 3-hydroxypyridinium derivatives, cyclopentenosine recently found in matured elastin, and in collagen, and pulcherosine a novel tyrosine-derived found in fertilization envelope of Sea Urchin embryo, di-tyrosine in resilin, gamma-glutamyl-lysine isopeptide cross-linking molecule etc. are listed and both physico-chemical and analytical methods are extensively reviewed and discussed. 4. Other consequences of post-translational modifications encountered in the analytical procedure such as N-terminal step-wise Edman degradation of glycosylated site(s), phosphorylated-site(s) and or sulfated-site(s) were also reported by us.
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Unité INSERM No. 16, Lille, France.
Martinage
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D006801:Humans; D008969:Molecular Sequence Data; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*
D000596:Amino Acids; D011506:Proteins