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Modification of aspartic acid residues to induce trypsin cleavage

✍ Scribed by Tusn-Tien Wang; N.Martin Young

Publisher: Elsevier Science
Year: 1978
Tongue: English
Weight: 240 KB
Volume: 91
Category: Article
ISSN: 0003-2697
DOI: 10.1016/0003-2697(78)90557-2

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✦ Synopsis

1,2-Diaminoethane and diaminomethane were coupled to aspartic acid residues in small peptides by means of a water-soluble carbodiimide. The resulting modified side chains sufficiently resembled lysine for trypsin to cleave the peptides. Similar modification of glutamic acid residues in peptides gave little or no susceptibility to trypsin.

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