H-Met-Gly-Met-Met-OH
H-Met-Gly-Met-Met-OH structure
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Common Name | H-Met-Gly-Met-Met-OH | ||
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| CAS Number | 14517-45-4 | Molecular Weight | 468.65500 | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | C17H32N4O5S3 | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
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Metal promiscuity and metal-dependent substrate preferences of Trypanosoma brucei methionine aminopeptidase 1.
Biochimie 115 , 35-43, (2015) Methionine aminopeptidases play a major role in posttranslational protein processing and are therefore promising targets for the discovery of novel therapeutical agents. We here describe the heterologous expression, purification, and characterization of recom... |
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Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity.
BMC Biochem. 12 , 35, (2011) Methionine aminopeptidase (MetAP) is a ubiquitous enzyme in both prokaryotes and eukaryotes, which catalyzes co-translational removal of N-terminal methionine from elongating polypeptide chains during protein synthesis. It specifically removes the terminal me... |
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Characterization of post-translationally modified peptides by hydrophilic interaction and reverse phase liquid chromatography coupled to quadrupole-time-of-flight mass spectrometry.
J. Chromatogr. A. 1428 , 202-11, (2016) This work explores the use of both hydrophilic interaction liquid chromatography (HILIC) and reverse phase liquid chromatography (RPLC) for the separation and subsequent characterization of bovine caseinomacropeptide (CMP) phosphopeptides and O-glycopeptides ... |
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Amino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity Kanudia et al.
BMC Biochem. 12 , online, (2011)
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