Endoproteinase Lys-C
Endoproteinase Lys-C structure
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Common Name | Endoproteinase Lys-C | ||
|---|---|---|---|---|
| CAS Number | 72561-05-8 | Molecular Weight | 509.552 | |
| Density | 1.3±0.1 g/cm3 | Boiling Point | 781.9±60.0 °C at 760 mmHg | |
| Molecular Formula | C30H27N3O5 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | 426.7±32.9 °C | |
| Symbol |
GHS07, GHS08 |
Signal Word | Danger | |
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Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
Anal. Chem. 81(11) , 4493-501, (2009) The analysis of proteome-wide phosphorylation events is still a major analytical challenge because of the enormous complexity of protein phosphorylation networks. In this work, we evaluate the complementarity of Lys-N, Lys-C, and trypsin with regard to their ... |
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Identification of the lysine residue responsible for coenzyme A binding in the heterodimeric 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus tokodaii, a thermoacidophilic archaeon, using 4-fluoro-7-nitrobenzofurazan as an affinity label
Biochim. Biophys. Acta 1794(2) , 335-40, (2009) The heterodimeric 2-oxoacid:ferredoxin oxidoreductase (StOFOR) from Sulfolobus tokodaii, a thermoacidophilic archaeon, was inactivated by low concentrations of 4-fluoro-7-nitrobenzofurazan (NBD-F), with concomitant increase in fluorescence in subunit-b. The i... |
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Proteomic analysis of annexin A2 phosphorylation induced by microtubule interfering agents and kinesin spindle protein inhibitors.
J. Proteome Res. 9 , 4649-4660, (2010) Microtubule interfering agents (MIAs) are antitumor drugs that inhibit microtubule dynamics, while kinesin spindle protein (KSP) inhibitors are substances that block the formation of the bipolar spindle during mitosis. All these compounds cause the accumulati... |
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Studying the fragmentation behavior of peptides with arginine phosphorylation and its influence on phospho-site localization.
Proteomics 13(6) , 945-54, (2013) Phospho-proteomic studies opened a broad view onto the main mechanisms of regulating cellular processes. Our recent discovery of a protein arginine kinase and its target in bacteria added a previously undescribed type of phosphorylation to control protein act... |
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Probing PrPSc structure using chemical cross-linking and mass spectrometry: evidence of the proximity of Gly90 amino termini in the PrP 27-30 aggregate.
Biochemistry 44(30) , 10100-9, (2005) Elucidation of the structure of PrP(Sc) continues to be one of the most important and difficult challenges in prion research. This task, essential for gaining an understanding of the basis of prion infectivity, has been hampered by the insoluble, aggregated n... |
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Determination of phosphorylated and O-glycosylated sites by chemical targeting (CTID) at ambient temperature.
Methods Mol. Biol. 386 , 79-93, (2007) In the analytical approach called chemically targeted identification (CTID), peptides containing phosphorylated or glycosylated serine and threonine underwent beta-elimination to produce an unsaturated double bond. Nucleophilic addition of 2-aminoethanethiol ... |
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Valence parity to distinguish c' and z• ions from electron capture dissociation/electron transfer dissociation of peptides: effects of isomers, isobars, and proteolysis specificity.
Anal. Chem. 83(20) , 8024-8, (2011) Valence parity provides a way to distinguish between N-terminal and C-terminal electron capture dissociation/electron transfer dissociation (ECD/ETD) product ions based on their number of hydrogen plus nitrogen atoms determined by accurate mass measurement an... |
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Posttranslational modifications of the bovine lens beaded filament proteins filensin and CP49.
Invest. Ophthalmol. Vis. Sci. 51(3) , 1565-1574, (2010) The lens beaded filament proteins filensin and CP49 are phosphorylated proteins that undergo proteolytic degradation with fiber cell age; however, the specific sites of modifications remain largely unknown. The purpose of this study was to identify posttransl... |
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Purification, cDNA cloning, and recombinant expression of chymotrypsin C from porcine pancreas.
Acta Biochim. Biophys. Sin. (Shanghai) 43(7) , 568-75, (2011) Chymotrypsin C is a bifunctional secretory-type serine protease in pancreas; besides proteolytical activity, it also exhibits a calcium-decreasing activity in serum. In this study, we purified activated chymotrypsin C from porcine pancreas, and identified its... |
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pH-dependent changes in photoaffinity labeling patterns of the H1 influenza virus hemagglutinin by using an inhibitor of viral fusion.
J. Virol. 73(3) , 1785-1794, (1999) The hemagglutinin (HA) protein undergoes a low-pH-induced conformational change in the acidic milieu of the endosome, resulting in fusion of viral and cellular membranes. A class of compounds that specifically interact with the HA protein of H1 and H2 subtype... |