期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 131, 期 31, 页码 10800-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja902681k
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资金
- National Institutes of Health [R01-AI057182, R01-AI033456, R21-EB008875]
- Fundacao para a Ciencia e Tecnologia (Portugal)
- MIT's Undergraduate Research Opportunities Program (UROP)
The unique reactivity of two sortase enzymes, SrtA(staph) from Staphylococcus aureus and SrtA(strep) from Streptococcus pyogenes, is exploited for site-specific labeling of a single polypeptide with different labels at its N and C termini. SrtA(strep) is used to label the protein's C terminus at an LPXTG site with a fluorescently labeled dialanine nucleophile. Selective N-terminal. labeling of proteins containing N-terminal glycine residues is achieved using SrtA(staph) and LPXT derivatives. The generality of N-terminal labeling with SrtA(staph) is demonstrated by near-quantitative labeling of multiple protein substrates with excellent site specificity.
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