English name: Carboxypeptidase Y from baker's yeast
Vitality: ≥50 units / mg protein
Dynamic definition of: One unit will hydrolyze 1.0 μmole of N-CBZ-Phe-Ala to N-CBZ-L-phenylalanine and L-alanine per min at pH 6.75 at 25 ° C, based on EM / 230 = 191.5
Product description: A glycoprotein exopeptidase of the acid and serine calss Highly purified specific activity in two different substrate systems:. Z-Phe-Leu, Z-Glu-Tyr.
Characters: White powder or solid, isoelectric point 3.6, the extinction coefficient A 280 nm of 15.0 enzyme may be diisopropyl fluorophosphate (DFP) inhibited, it can also be to some metal ions such as Cu2 +, Hg2 +, Fe2 + , Mg2 +, etc. suppression
Use: Biochemical studies can begin to degrade specificity from the C-terminus of the peptide chain individually, releasing free amino acids of a class of peptides exonuclease zymogen form in vivo carboxypeptidase Y of the terminal carboxyl groups. various amino acids have a wide range of hydrolysis, so the enzyme has become a polypeptide chain C-terminal protein analysis tools commonly used enzyme, and pancreatic carboxypeptidase A and B are not the same, it is a non-metal ions acidic protein, having peptidase and lipase activity
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