Get paper from

journal cover

Determination of carboxypeptidase A using N-acetyl-phenylalanyl-3-thiaphenylalanine as substrate: application to a direct serum assay

Analytical Biochemistry

Feb 15, 1987

Kyle BrownCharles Gilvarg

PMID: 3578784

Get paper from

Abstract

N-Acetyl-L-phenylalanyl-L-3-thiaphenylalanine has been shown to be a substrate for carboxypeptidase A. Hydrolysis of the compound obeys Michaelis-Menten kinetics with a KM of 0.22 mM and a kcat of 6720 min-1 at 22 degrees C. A colorimetric assay, employing Ellman's reagent to detect the...read more

Mentioned in this Paper

Phenylalanyl-3-thiaphenylalanine
Thiophenol
Substrate Specificity
Hydrolysis
Carboxypeptidase A5
Dithionitrobenzoic Acid
Colorimetry
Carboxypeptidase A Activity
Cytokinesis of the Fertilized Ovum
Cytokinesis
Paper Details
References

Determination of carboxypeptidase A using N-acetyl-phenylalanyl-3-thiaphenylalanine as substrate: application to a direct serum assay

Analytical Biochemistry

Feb 15, 1987

Kyle BrownCharles Gilvarg

PMID: 3578784

DOI:

Abstract

N-Acetyl-L-phenylalanyl-L-3-thiaphenylalanine has been shown to be a substrate for carboxypeptidase A. Hydrolysis of the compound obeys Michaelis-Menten kinetics with a KM of 0.22 mM and a kcat of 6720 min-1 at 22 degrees C. A colorimetric assay, employing Ellman's reagent to detect the...read more

Mentioned in this Paper

Phenylalanyl-3-thiaphenylalanine
Thiophenol
Substrate Specificity
Hydrolysis
Carboxypeptidase A5

Related Papers

Paper Details
References

Get paper from

/papers/determination-of-carboxypeptidase-a-using-n-acetyl/3578784