| 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. | |
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MedLine Citation:
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PMID: 8365549 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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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Authors:
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K K Han; A Martinage |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review |
Journal Detail:
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Title: The International journal of biochemistry Volume: 25 ISSN: 0020-711X ISO Abbreviation: Int. J. Biochem. Publication Date: 1993 Jul |
Date Detail:
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Created Date: 1993-10-05 Completed Date: 1993-10-05 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0250365 Medline TA: Int J Biochem Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 957-70 Citation Subset: IM |
Affiliation:
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Unité INSERM No. 16, Lille, France. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Amino Acids / chemistry, metabolism* Animals Humans Molecular Sequence Data Protein Processing, Post-Translational* Proteins / metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Amino Acids; 0/Proteins |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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