N-CBZ-Phe-Leu (Z-phe-Ieu) (CBZ-phenylalanylleucine) is an N-terminal protected Cbz-dipeptide substrate used to differentiate, characterize and kinetically analyze various carboxypeptidase(s).
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Journal of agricultural and food chemistry, 49(10), 5019-5030 (2001-10-16)
The hepatopancreas of squid (Illex illecebrosus) extract contains a wide range of carboxypeptidase (CP) activities based on hydrolysis of N-CBZ-dipeptide substrates. SDS-PAGE zymograms with N-CBZ-Phe-Leu substrate revealed three activity zones (CP-I, 23 kDa; CP-II, 29 kDa; CP-III, 42 kDa). CP-I
Human platelets were investigated for activity of the acidic carboxypeptidases: cathepsin A, lysosomal carboxypeptidase B and prolyl-carboxypeptidase. It was found that the main acidic carboxypeptidase in human platelets had cathepsin A activity. No activity of lysosomal carboxypeptidase B and prolyl-carboxypeptidase
Journal of biotechnology, 128(2), 322-334 (2006-11-30)
The gene encoding a Deinococcus radiodurans R1 bifunctional aminoacylase/carboxypeptidase (DR_ACY/CP) was amplified by polymerase chain reaction and cloned into pQE-30 to generate pQE-DRAC. The cloned gene consists of an open reading frame of 1197 bp encoding a protein with a
European journal of biochemistry, 269(13), 3220-3225 (2002-06-27)
Cys341 of carboxypeptidase Y, which constitutes one side of the solvent-accessible surface of the S1 binding pocket, was replaced with Gly, Ser, Asp, Val, Phe or His by site-directed mutagenesis. Kinetic analysis, using Cbz-dipeptide substrates, revealed that polar amino acids
Journal of industrial microbiology & biotechnology, 35(1), 41-47 (2007-10-19)
Effects of the enzymes in Actinomucor elegans extract and the enzyme Alcalase 2.4L on debittering the soybean protein hydrolysates were investigated. When the protein was treated only with the latter, a strong bitterness formed; but it decreased if the protein
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