Results 171 to 180 of about 6,217 (212)
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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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Immunochemical studies on carboxypeptidase A
Immunochemistry, 1965Abstract Rabbit antibodies to carboxypeptidase A (CPA) were characterized by various immunochemical techniques including double diffusion in agar, enzyme inhibition and complement fixation. Procarboxypeptidase A (PCPA), the zymogen, contains two other subunits in addition to the precursor of CPA. PCPA reacts with antiCPA but less effectively than
H I, Lehrer, H, Van Vunakis
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Binding of Zinc in Carboxypeptidase
Nature, 1960CARBOXYPEPTIDASE is a metallo-enzyme which contains zinc. It has been reported by Coleman and Vallee1 that the enzyme can be de-activated by removal of zinc and that activity can be restored by the addition of zinc, cobaltous, ferrous, nickel and manganous ions but not by addition of cadmium, magnesium or calcium ions.
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