Sequence determination of lychnin, a type 1 ribosome-inactivating protein from Lychnis chalcedonica seeds
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Angela Chambery
Abstract
The complete amino acid sequence of lychnin, a type 1 ribosome-inactivating protein (RIP) isolated from Lychnischalcedonica seeds, has been determined by automated Edman degradation and ESI-QTOF mass spectrometry. Lychnin consists of 234 amino acid residues with a molecular mass of 26 131.14 Da. All amino acid residues involved in the formation of the RIP active site (Tyr69, Tyr119, Glu170, Arg173 and Trp203) are fully conserved. Furthermore, a fast MALDI-TOF experiment showed that two out of three cysteinyl residues (Cys32 and Cys115) form a disulfide bridge, while Cys214 is in the thiol form, which makes it suitable for linking carrier molecules to generate immunotoxins and other conjugates.
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©2006 by Walter de Gruyter Berlin New York
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Articles in the same Issue
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- The aryl hydrocarbon receptor and light
- The impact of aryl hydrocarbon receptor signaling on matrix metabolism: implications for development and disease
- A role for the aryl hydrocarbon receptor in mammary gland tumorigenesis
- Evidence supporting the hypothesis that one of the main functions of the aryl hydrocarbon receptor is mediation of cell stress responses
- The arylhydrocarbon receptor repressor (AhRR): structure, expression, and function
- Impact of the arylhydrocarbon receptor on eugenol- and isoeugenol-induced cell cycle arrest in human immortalized keratinocytes (HaCaT)
- Aryl hydrocarbon receptor agonists directly activate estrogen receptor α in MCF-7 breast cancer cells
- Identifying target genes of the aryl hydrocarbon receptor nuclear translocator (Arnt) using DNA microarray analysis
- Transcriptional signatures of immune cells in aryl hydrocarbon receptor (AHR)-proficient and AHR-deficient mice
- 14-3-3 proteins in membrane protein transport
- The K+ channel gene, Kcnb1: genomic structure and characterization of its 5′-regulatory region as part of an overlapping gene group
- Structure-based specificity mapping of secreted aspartic proteases of Candida parapsilosis, Candida albicans, and Candida tropicalis using peptidomimetic inhibitors and homology modeling
- The solution structure of the membrane-proximal cytokine receptor domain of the human interleukin-6 receptor
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