C1261
Carboxypeptidase A−Agarose
ammonium sulfate suspension, ≥6 units/mL packed gel, 25 °C, enzyme from bovine pancreas
Synonym(s):
Carboxypolypeptidase, Peptidyl-L-amino-acid hydrolase
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About This Item
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Recommended Products
biological source
enzyme from bovine pancreas
Quality Level
form
ammonium sulfate suspension
specific activity
≥6 units/mL packed gel, 25 °C
mol wt
~35,250
matrix
beaded agarose
storage temp.
2-8°C
General description
Carboxypeptidase A-agarose product is prepared by the immobilization of carboxypeptidase A, originally isolated from the bovine pancreas, to activated 4% crosslinked beaded agarose.
Biochem/physiol Actions
Carboxypeptidase as isolated from bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by β-phenylpropionate and indole acetate.
Carboxypeptidase A is attached covalently to agarose or aldehyde and is effective for immobilization studies.
Unit Definition
One unit will hydrolyze 1.0 μmole of hippuryl-L-phenylalanine per min at pH 7.5 at 25 °C.
Physical form
Suspension in 2.0 M (NH4)2SO4, pH 7
inhibitor
Product No.
Description
Pricing
substrate
Product No.
Description
Pricing
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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Sahar I Da'as et al.
Blood, 119(15), 3585-3594 (2012-03-01)
We used the opportunities afforded by the zebrafish to determine upstream pathways regulating mast cell development in vivo and identify their cellular origin. Colocalization studies demonstrated zebrafish notch receptor expression in cells expressing carboxypeptidase A5 (cpa5), a zebrafish mast cell-specific
Hilana Salete Silva Oliveira et al.
Journal of food science, 76(5), C755-C759 (2012-03-16)
This paper proposes a method to enzymatically treat poor-quality cocoa almonds (known as "slate") to ensure the formation of chocolate flavor precursors. The production of flavor precursors improves the quality of these almonds, which are usually responsible for the low
Sandeep Chakraborty et al.
PloS one, 7(2), e32011-e32011 (2012-02-24)
Promiscuity, the basis for the evolution of new functions through 'tinkering' of residues in the vicinity of the catalytic site, is yet to be quantitatively defined. We present a computational method Promiscuity Indices Estimator (PROMISE)--based on signatures derived from the
Zhenhua Li et al.
BMC bioinformatics, 13, 51-51 (2012-03-29)
Water is an integral part of protein complexes. It shapes protein binding sites by filling cavities and it bridges local contacts by hydrogen bonds. However, water molecules are usually not included in protein interface models in the past, and few
Arthur A Topilow et al.
Cancer biomarkers : section A of Disease markers, 10(1), 27-33 (2012-02-03)
Pancreatic cancer has a dismal prognosis because it is often diagnosed at an advanced stage. Therefore, serological biomarkers are eagerly sought for early detection. The digestive enzyme pro-carboxypeptidase A (PCPA) may be able to fill this role. The purpose of
Protocols
Enzymatic Assay of Carboxypeptidase
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