Results 211 to 220 of about 41,156 (268)
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2014
Threonine aldolases catalyze the pyridoxal phosphate-dependent condensation between small amino acids (principally glycine) and aldehydes such as acetaldehyde. Carbon-carbon bond formation involves forming two adjacent chiral centers. As a rule, threonine aldolases are very stereoselective for α-carbon configuration but show modest selectivity at the β-
Sarah E, Franz, Jon D, Stewart
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Threonine aldolases catalyze the pyridoxal phosphate-dependent condensation between small amino acids (principally glycine) and aldehydes such as acetaldehyde. Carbon-carbon bond formation involves forming two adjacent chiral centers. As a rule, threonine aldolases are very stereoselective for α-carbon configuration but show modest selectivity at the β-
Sarah E, Franz, Jon D, Stewart
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Science, 1966
A new method of starch-gel electrophoresis using a technique of staining dependent on enzyme activity has been employed to demonstrate the isozymes of aldolase from a variety of human, rat, and frog tissues. Five of these isozymes were detected in man, seven in the rat, and at least four in the frog. The abilities of these isozymes to cleave fructose-1,
H B, Anstall, C, Lapp, J M, Trujillo
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A new method of starch-gel electrophoresis using a technique of staining dependent on enzyme activity has been employed to demonstrate the isozymes of aldolase from a variety of human, rat, and frog tissues. Five of these isozymes were detected in man, seven in the rat, and at least four in the frog. The abilities of these isozymes to cleave fructose-1,
H B, Anstall, C, Lapp, J M, Trujillo
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Threonine Aldolase and Allothreonine Aldolase in Rat Liver
European Journal of Biochemistry, 19691 The aldol breakdown of l-threonine and l-allothreonine in rat liver is catalyzed by systems localized in the soluble fraction of the homogenate. 2 Evidence in presented that two different enzymes, indicated as “threonine aldolase” and “allothreonine aldolase”, are involved in the breakdown of the two amino ...
G, Riario-Sforza +2 more
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Zeitschrift f�r Krebsforschung, 1959
The enzyme aldolase is isolated and crystallized from human breast tumor. The purification of the enzyme involved methanol fractionation, exposure to a temperature of 38°C, adsorption and elution from aluminium hydroxide gel, and precipitation followed by crystallization from ammonium sulfate.
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The enzyme aldolase is isolated and crystallized from human breast tumor. The purification of the enzyme involved methanol fractionation, exposure to a temperature of 38°C, adsorption and elution from aluminium hydroxide gel, and precipitation followed by crystallization from ammonium sulfate.
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Rinsho byori. The Japanese journal of clinical pathology, 2002
Aldolase (EC 4.1.2.13) plays an important role in glucose metabolism. Aldolase has a molecular weight of 160 kDa and has three isozymes, namely aldolase A, B and C. The enzyme is probably present in all cells; it occurs in particularly large quantities in the muscles, liver and brain. An increase in serum aldolase is found in myotonic muscular disease,
K, Taguchi, Y, Takagi
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Aldolase (EC 4.1.2.13) plays an important role in glucose metabolism. Aldolase has a molecular weight of 160 kDa and has three isozymes, namely aldolase A, B and C. The enzyme is probably present in all cells; it occurs in particularly large quantities in the muscles, liver and brain. An increase in serum aldolase is found in myotonic muscular disease,
K, Taguchi, Y, Takagi
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Science, 1971
A new crystal form of rabbit muscle aldolase shows that the molecule has 222 symmetry to at least 4-angstrom resolution, and hence that the gross conformation of the four subunits is the same. Comparison of the new form with a previously reported form establishes the number of molecules per unit cell, n , in the ...
E G, Heidner, B H, Weber, D, Eisenberg
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A new crystal form of rabbit muscle aldolase shows that the molecule has 222 symmetry to at least 4-angstrom resolution, and hence that the gross conformation of the four subunits is the same. Comparison of the new form with a previously reported form establishes the number of molecules per unit cell, n , in the ...
E G, Heidner, B H, Weber, D, Eisenberg
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Liver aldolase anomeric specificity
Biochemistry, 1980Stopped-flow kinetic studies of liver aldolase and of mixed liver-muscle aldolase catalyzed reactions of fructose 1,6-bisphosphate (FBP) have been carried out and interpreted by computer simulation. These experiments indicate no utilization or binding of the alpha anomer by the liver enzyme unlike the findings for either the muscle aldolase which binds
K J, Schray +4 more
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Directed Evolution of Aldolases
2004Publisher Summary This chapter describes the directed evolution of aldolases. The detailed protocols for generating aldolases with new catalytic properties are presented. The gene encoding aldolase can be amplified using the standard polymerase chain reaction (PCR) from a genomic DNA preparation using the Qiagen kit and primers flanking the gene with
Dirk, Franke +2 more
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Tagatose‐1,6‐Bisphosphate Aldolases, the Unloved DHAP‐Aldolases
ChemBioChemTagatose‐1,6‐bisphosphate aldolases (TagA) have been understudied. The limited publications on the subject report a poor stereoselectivity, which quickly leads to their classification among the less interesting aldolases. This conclusion, which appears inadequate, discourages further investigation by other researchers.
Léo Paulat +3 more
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Predicted structure for aldolase
Journal of Molecular Biology, 1976Abstract Recent chromatographic and absorbance spectral measurements using the dye Cibacron blue F3GA (Stellwagen et al., 1975) have indicated that the substrate-binding site of fructose diphosphate aldolase is constructed by a supersecondary structural array closely resembling the NAD-domain commonly found in a variety of glycolytic enzymes ...
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