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Isozymes of Aldolase

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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Threonine Aldolase and Allothreonine Aldolase in Rat Liver

European Journal of Biochemistry, 1969
1 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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Threonine Aldolases

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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Radioimmunoassay for human aldolase A

Clinica Chimica Acta, 1981
A radioimmunoassay was developed for the direct quantification of aldolase A in human serum. The method is a double antibody radioimmunoassay using radioiodinated aldolase A4 homopolymer as ligand, chicken antibodies to aldolase A, and rabbit antibodies to chicken IgG. The lowest measurable amount by this method was 2 ng (0.01 U).
M, Asaka   +4 more
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Subunit Structure of Aldolase

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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