Results 141 to 150 of about 5,330 (195)
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Annual Review of Physiology, 1988
Carboxypeptidase E appears to be involved in the biosynthesis of a wide range of peptide hormones and neurotransmitters. The evidence for this is: (a) CPE is present in tissues that produce bioactive peptides; (b) in tissues that have been subjected to subcellular fractionation, the CPE activity is associated with peptide-containing secretory granules;
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Carboxypeptidase E appears to be involved in the biosynthesis of a wide range of peptide hormones and neurotransmitters. The evidence for this is: (a) CPE is present in tissues that produce bioactive peptides; (b) in tissues that have been subjected to subcellular fractionation, the CPE activity is associated with peptide-containing secretory granules;
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Cleavage of the carboxypeptidase inhibitor from potatoes by carboxypeptidase A
Biochemical and Biophysical Research Communications, 1980Summary The association of carboxypeptidase A with the carboxypeptidase inhibitor from potatoes results in the rapid removal of the carboxyl-terminal glycine residue from the inhibitor. At an equimolar concentration of inhibitor and enzyme, the half-time for hydrolysis is approximately thirty seconds at pH 7.5.
G M, Hass, C A, Ryan
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Dynamical structure of carboxypeptidase A
Journal of Molecular Biology, 1989Structural fluctuations of the apoenzyme form of carboxypeptidase A (EC 3.4.12.2) have been evaluated on the basis of molecular dynamics. The Konnert-Hendrickson refined coordinates of 2437 non-hydrogen atoms of the 307 amino acid residues derived from the X-ray structure of the holoenzyme served as the molecular model together with 548 calculated ...
MAKINEN, MW +4 more
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1974
In this article the main theme to be discussed will be our continuing studies on the mechanism of action of the zinc-containing metalloenzyme bovine carboxypeptidase A. A summary of earlier mechanistic studies in our laboratory on carboxypeptidase A was published recently (Kaiser and Kaiser, 1972).
E T, Kaiser, T W, Chan, J, Suh
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In this article the main theme to be discussed will be our continuing studies on the mechanism of action of the zinc-containing metalloenzyme bovine carboxypeptidase A. A summary of earlier mechanistic studies in our laboratory on carboxypeptidase A was published recently (Kaiser and Kaiser, 1972).
E T, Kaiser, T W, Chan, J, Suh
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2013
The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 850 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing
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The third edition of the Handbook of Proteolytic Enzymes aims to be a comprehensive reference work for the enzymes that cleave proteins and peptides, and contains over 850 chapters. Each chapter is organized into sections describing the name and history, activity and specificity, structural chemistry, preparation, biological aspects, and distinguishing
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Carboxypeptidase inhibitor from potatoes. Interaction with derivatives of carboxypeptidase A
Biochemistry, 1976The mechanism of action of a carboxypeptidase inhibitor from potatoes has been probed by studying its interaction with derivatives of carboxypeptidase A containing modified residues at the active site. Arsanilazocarboxypeptidase A, a derivative containing a chromophore attached to tyrosine 248, exhibits a circular dichroism spectrum which is sensitive ...
H, Ako +3 more
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Biokhimiia (Moscow, Russia), 1984
Carboxypeptidase T, an extracellular carboxypeptidase from Thermoactinomyces sp. was isolated and purified by affinity chromatography on bacitracin adsorbents. The enzyme homogeneity was established by SDS electrophoresis (Mr = 38 000) and isoelectrofocusing in PAAG (pI 5.3).
A L, Osterman +4 more
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Carboxypeptidase T, an extracellular carboxypeptidase from Thermoactinomyces sp. was isolated and purified by affinity chromatography on bacitracin adsorbents. The enzyme homogeneity was established by SDS electrophoresis (Mr = 38 000) and isoelectrofocusing in PAAG (pI 5.3).
A L, Osterman +4 more
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