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Microidentification of N-Terminal-Blocked Amino Acid Residues of Proteins and Peptides

✍ Scribed by Y. Kawakami; S. Ohmori

Publisher: Elsevier Science
Year: 1994
Tongue: English
Weight: 540 KB
Volume: 220
Category: Article
ISSN: 0003-2697
DOI: 10.1006/abio.1994.1300

No coin nor oath required. For personal study only.

✦ Synopsis

Proteins or peptides having an (\mathrm{N})-terminal-blocked amino acid were successively digested by pronase (E), proteinase (K), and carboxypeptidase (Y). The (\mathbf{N})-blocked amino acids released from proteins or peptides were derivatized with 9 -anthryldiazomethane (ADAM) to the corresponding esters followed by addition of formic acid to remove the remaining ADAM which interfered with further analysis. The anthryl esters were analyzed by high-performance liquid chromatography equipped with a fluorimetric detector. Twelve (N)-acetylamino acids (Asn, Gln, Ser, Thr, Gly, Ala, Tyr, Pro, Met, Val, Ile, and Leu), pyroglutamic acid, (\boldsymbol{N})-formylMet, and (\boldsymbol{N}) myristoylGly could be separated from each other and identified on the same chromatographic run. As examples of applied experiments to proteins and peptides, (\mathrm{N})-acetyl derivatives of Ser, Ala, Met, Gly, Tyr, and Pro as well as (\boldsymbol{N})-myristoylGly could be satisfactorily identified using (100 \mathrm{pmol}) each of seven proteins and peptides. The method reported here is an improved one that was reported in the previous paper based on the same principles. 1994 Academic Press, Inc.

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