Hippuryl-L-phenylalanine has been used as a substrate for screening carboxypeptidase activity in Trogoderma granarium,[1]Bactrocera oleae Gmelin[2] and Apodiphus amygdali.[3]
Biochem/physiol Actions
Hippuryl-L-phenylalanine is a substrate for carboxypeptidase A enzyme.[4]
This paper presents stable carboxypeptidase A (CPA)-glyoxyl derivatives, to be used in the controlled hydrolysis of proteins. They were produced after immobilizing-stabilizing CPA on cross-linked 6% agarose beads, activated with low and high concentrations of aldehyde groups, and different immobilization
Digestion and protein metabolism of Trogoderma granarium (Coleoptera: Dermestidae) fed on different barley varieties
Mardani-Talaee M, et al.
Journal of Stored Products Research, 73(1-2), 37-41 (2017)
Biochemical and biophysical research communications, 132(2), 681-687 (1985-10-30)
Carboxypeptidase A was incubated at -60 degrees C with an excess of O-(trans-p-chlorocinnamoyl)-L-phenyllactate, O-(hippuryl)-glycolate or N-(hippuryl)-L-phenylalanine. After rapid denaturation with trichloracetic acid the precipitated protein was reduced with [3H]NaCNBH3. 3H Labeled enzyme was isolated by gel chromatography on Sephadex G-25.
Product stabilization of the two forms of carboxypeptidase A from buffalo pancreas
Carboxypeptidase A activity measured via continuous spectrophotometric rate determination assay with hippuryl-L-phenylalanine substrate.
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