Results 271 to 280 of about 471,402 (314)
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Aspartate–Glutamate Transaminase in a Red Halophilic Bacterium
Nature, 1953LITTLE information is available on the metabolism of the red halophilic bacteria, although they represent a most interesting ecological group of organisms and are of some importance in the packing, pickling and curing industries. In a survey of their respiratory activity it was observed that resting cells did not oxidize readily the common carbon ...
J, ROBINSON, H, KATZNELSON
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The N-terminal groups of glutamic aspartic transaminase
Experientia, 1962Su una preparazione altamente purificata di glutammico aspartico transaminasi del cuore di porco sono stati determinati i gruppi N-terminali con il metodo diSanger. E stata dimostrata la presenza di una mole di alanina N-terminale per 58 000 g di proteina, cioe per una mole di coenzima.
C, TURANO, P, VECCHINI, A, GIARTOSIO
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Aspartate aminotransferase in Leishmania is a broad-spectrum transaminase
Transactions of the Royal Society of Tropical Medicine and Hygiene, 1984The substrate specificity of aspartate aminotransferase (ASAT, E.C. 2.6.1.1.) from Leishmania was examined following observations of artefacts on gels stained for alanine aminotransferase (ALAT, E.C. 2.6.1.2.) after thin-layer starch-gel electrophoresis. Leishmanial ASAT acted on L-aspartate, L-alanine, L-tryptophan and L-tyrosine.
S M, Le Blancq, S M, Lanham
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Glutamic‐Aspartic Transaminase — Antitransaminase Interaction:
European Journal of Biochemistry, 1969Transaminase was cross‐linked with various proteins after the addition of glutaraldehyde or ethyl chloroformate. The water insoluble conjugates were used for the purification of antitransaminase and antiapotransaminase. A method is described. Pig heart transaminase and ox heart transaminase react differently with anti‐pig‐heart transaminase and ...
I, Patramani +5 more
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Reversible dissociation of succinylated aspartate transaminase into subunits
Biochemical and Biophysical Research Communications, 1965Abstract The molecule of succinylated aspartate-transaminase (mol. weight 117,000) dissociates into two subunits in alkaline solutions. Upon reneutralization to pH 6.5 the enzyme subunits reassociate. In the region of pH-optimum (pH 8.5–9.3) succinylated transaminase retains 65 per cent of the catalytic activity of native transaminase.
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Aspartate transaminases are required for blood development
Abstract Red blood cells (RBCs) have a limited lifespan of approximately 120 days. This necessitates continuous RBC production, resulting in ∼200 billion new RBCs made per day to maintain oxygen delivery. Despite this enormous biosynthetic demand, the metabolic pathways supporting erythropoiesis are poorly understood.Narges Pourmandi +21 more
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Circular dichroism of aspartate transaminase
Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964Y N, BREUSOV +3 more
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On the acetylation of glutamic aspartic transaminase
Archives of Biochemistry and Biophysics, 1962C, TURANO, A, GIARTOSIO, P, VECCHINI
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