Abstract
Background:Proteolysis constitutes a major post-translational modification. For example, proteases regulate the activation or inactivation of various proteins, such as enzymes, growth factors, and peptide hormones. Proteases have substrate specificity, and protease expression regulates the specific and regional activation or inactivation of several functional proteins.Methods:We demonstrate a novel method for determining protease specificity through the use of MALDI-TOF mass spectrometry with biotin-labeled substrates.Results:This method was able to determine the specificity of TPCK-trypsin, V8 protease, elastase and cyanogen bromide cleavage, and the results were similar to previous reports. In addition, the method can be used to measure crude samples, such as tumor extracts.Conclusion:We demonstrated that this method could identify protease specificity after simple processing, even for crude samples.
Highlights
We demonstrated that this method could identify protease specificity after simple processing, even for crude samples
Most proteins are activated by post-translational modifications, such as glycosylation, phosphorylation, and proteolysis
This method used a set of peptide mixtures in which each of the 20 amino acid residues was systematically substituted at the protease cleavage site
Summary
Most proteins are activated by post-translational modifications, such as glycosylation, phosphorylation, and proteolysis. One method of controlling the activity of proteins is through specific protease cleavage sites. Proteases recognize specific amino acid sequences and conformations of substrates and subsequently cleave them. Identification of this specificity is important for understanding the function and mechanism of proteases. Proteases regulate the activation or inactivation of various proteins, such as enzymes, growth factors, and peptide hormones. Protease expression regulates the specific and regional activation or inactivation of several functional proteins
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