{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,19]],"date-time":"2025-09-19T10:42:08Z","timestamp":1758278528258},"reference-count":0,"publisher":"Portland Press Ltd.","issue":"2","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[1980,5,1]]},"abstract":"<jats:p>BNPS-skatole (3-bromo-3-methyl-2-(2-nitrophenyl)thiol-3H-indole) and N-bromosuccinimide have been used to specifically cleave at peptide bonds after amino acids with available C-gamma=C-delta double bonds, i.e. tryptophan, tyrosine and histidine. The resulting C-terminal lactones conveniently attach to amino-glass supports for sequencing with DABITC (4-NN-dimethylaminoazobenzene 4\u2032-isothiocyanate). Also, peptides having such C-termini, i.e. from a chymotryptic digest, can be readily made to react with these reagents and thus be easily attached and sequenced by solid-phase methods.<\/jats:p>","DOI":"10.1042\/bj1870515","type":"journal-article","created":{"date-parts":[[2015,8,10]],"date-time":"2015-08-10T20:22:05Z","timestamp":1439238125000},"page":"515-519","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["Peptide fragmentation suitable for solid-phase microsequencing. Use of <i>N<\/i>-bromosuccinimide and BNPS-skatole {3-bromo-3-methyl-2-[(2-nitrophenyl)thio]-3<i>H<\/i>-indole}"],"prefix":"10.1042","volume":"187","author":[{"given":"P E","family":"Hunziker","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"G J","family":"Hughes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"K J","family":"Wilson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","container-title":["Biochemical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/187\/2\/515\/574074\/bj1870515.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemj\/article-pdf\/187\/2\/515\/574074\/bj1870515.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,26]],"date-time":"2021-11-26T13:53:55Z","timestamp":1637934835000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemj\/article\/187\/2\/515\/5462\/Peptide-fragmentation-suitable-for-solid-phase"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1980,5,1]]},"references-count":0,"journal-issue":{"issue":"2","published-print":{"date-parts":[[1980,5,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bj1870515","relation":{},"ISSN":["0264-6021"],"issn-type":[{"type":"print","value":"0264-6021"}],"subject":[],"published":{"date-parts":[[1980,5,1]]}}}