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.

References

• 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.

* Immobilized Carboxypeptidase Y and other proteases are available in bulk quantities for manufacturing applications.