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N-Glycosylation patterns in two alpha-L-arabinofuranosidases from Penicillium canescens belonging to the glycoside hydrolase families 51 and 54статья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 4 февраля 2014 г.
- Авторы: Gusakov A.V., Sinitsyna O.A., Rozhkova A.M., Sinitsyn A.P.
- Журнал: Carbohydrate Research
- Том: 382
- Год издания: 2013
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 71
- Последняя страница: 76
- DOI: 10.1016/j.carres.2013.08.026
- Аннотация: Using MALDI-TOF mass spectrometry (MS) peptide fingerprinting procedure followed by the analysis of MS data with the GlycoMod tool from the ExPASy proteomic site, N-glycosylation of two GH51 and GH54 family alpha-L-arabinofuranosidases (Abf51A and Abf54A) from Penicillium canescens was studied. Variable N-linked glycans were identified at five out of eight potential N-glycosylation sites in the Abf51A and one out of three potential N-glycosylation sites in the Abf54A. The discriminated glycans represented high-mannose oligosaccharides (Man)x(GlcNAc)2 with a number of Man residues up to 7 or the products of sequential enzymatic trimming of a high-mannose glycan with alpha-mannosidases and beta-N-acetylhexosaminidases. The Abf54A peptide, containing the Asn254 glycosylation site, and one peptide from the Abf51A, containing the Asn163 glycosylation site, were found to exist not only in glycosylated, but also in a native non-modified form.
- Добавил в систему: Гусаков Александр Васильевич