Thermo Scientific Pierce Carboxypeptidase Y is a protease with that is able to cleave (release) any terminal amino acid including proline from the C-terminus of peptides; the immobilized form allows sample separation after treatment.
Carboxypeptidase Y is a glycoprotein exopeptidase of the serine class. Carboxypeptidase Y has a broad amino acid specificity, and is able to release every amino acid including proline from the carboxyl-terminus of peptides, although glycine and aspartic acid are released much more slowly than other residues. It is active in urea and SDS solutions and retains its activity under the denaturing conditions used for polypeptide sequencing.
Immobilized carboxypeptidase Y can be substituted for free carboxypeptidase Y in any application, and is advantageous because it virtually eliminates autolysis, eliminates contamination of a sample with the protease and allows control of the digestion by removing the carboxypeptidase Y. Immobilized carboxypeptidase Y is also more stable against heat-induced denaturation, resulting in longer maintenance of activity.
|Properties of Carboxypeptidase Y.
||Proteinase C, yeast carboxypeptidase Y
||Cleaves residues sequentially from the carboxy terminus
||S. cerevisiae (bakers yeast)
||Peptide hydrolysis for sequencing
||pH 5.5-7.5, 25°C
||Store carboxypeptidase Y and Immobilized carboxypeptidase Y at -20°C
||PMSF and DFP
||One unit of carboxypeptidase Y hydrolyzes one µmol of benzyl-oxycarbonyl-L-phenylalanyl-L-leucine per minute at 25°C, pH 6.5
- Hayashi, R. et al. (1973) Carboxypeptidase from Yeast. Large scale preparation and the application to COOH-terminal analysis of peptides and proteins. J. Bio. Chem. 248 , 2296-2302.
- Martin, B., et al. (1977) Carlsberg Res. Comm.42, 99-102.
- Stennicke, H., et al. (1996) Studies on the Hydrolytic Properties of (Serine) Carboxypeptidase Y. Biochem. 35, 7131.
All proteases and protein-cleaving reagents (including mass spectrometry-grade)
Mass spectrometry reagents and kits for proteomics