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Carboxypeptidase Y and Immobilized Carboxypeptidase Y


Sequentially removes amino acids from the C-terminus.

Pierce Carboxypeptidase Y

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.
Alternative names Proteinase C, yeast carboxypeptidase Y
Specificity Cleaves residues sequentially from the carboxy terminus
Source S. cerevisiae (bakers yeast)
Molecular weight 61,000
Protease type Serine exopeptidase
Uses/applications Peptide hydrolysis for sequencing
Reaction conditions  pH 5.5-7.5, 25°C
Storage conditions  Store carboxypeptidase Y and Immobilized carboxypeptidase Y at -20°C
Inhibitors PMSF and DFP
Unit definition One unit of carboxypeptidase Y hydrolyzes one µmol of benzyl-oxycarbonyl-L-phenylalanyl-L-leucine per minute at 25°C, pH 6.5

References:

  1. 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.
  2. Martin, B., et al. (1977) Carlsberg Res. Comm.42, 99-102.
  3. Stennicke, H., et al. (1996) Studies on the Hydrolytic Properties of (Serine) Carboxypeptidase Y. Biochem. 35, 7131.

Related Products:

Pierce Trypsin, MS Grade (Part No. 90057)
MS-Grade Proteases and Digestion Kits for Mass Spectrometry
Standard-Grade Proteases and Protease Resins
Enzymes for Cell Lysis


Ordering Information
 
Product # Description Pkg. Size Instructions MSDS CofA Price
20212 Carboxypeptidase Y
Formulation: Lyophilized enzyme in 0.1M sodium citrate, pH 5.3
Sufficient For: Approx. 130 units of activity/mg
1mg Product Instructions for product #20212 Carboxypeptidase Y MSDS for product #20212 Carboxypeptidase Y Certificate of Analysis for product #20212 Carboxypeptidase Y $189.00

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20236 Immobilized Carboxypeptidase Y
Formulation: Carboxypeptidase Y on crosslinked 4% beaded agarose, slurried in 50% glycerol with sodium azide
Sufficient For: At least 12.5 units of activity/mL resin
2mL MSDS for product #20236 Immobilized Carboxypeptidase Y Certificate of Analysis for product #20236 Immobilized Carboxypeptidase Y $219.00

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Instructions | MSDS | CofA
Product Instructions | MSDS | CofA  

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