Results 291 to 300 of about 472,544 (350)

Reconstituted aspartate aminotransferase physical studies

Biochimica et Biophysica Acta (BBA) - Enzymology, 1968
Abstract Apo-aspartate aminotransferase ( l -aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) from pig heart can be recombined with pyridoxal 5-phosphate to form reconstituted species with properties indistinguishable from those of the original enzyme. Two distinct types of enzyme properties were investigated in these studies.
J G, Farrelly, J E, Churchich
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Macro-aspartate aminotransferase and pregnancy

European Journal of Gastroenterology & Hepatology, 2004
Macro-aspartate aminotransferase (AST) is a benign condition characterised by unexplained persistent fluctuations f this macroenzyme complex in serum. However, it is not clear what causes this phenomenon or which factors favour its appearance in the blood. Moreaover, it is not known whether normal pregnancy mayinfluence macro-AST levels or whether this
ORLANDO, ROCCO, LIRUSSI F.
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Inhibition of aspartate aminotransferase by hydrazinosuccinate

Biochimica et Biophysica Acta (BBA) - General Subjects, 1984
DL-Hydrazinosuccinic acid was synthesized by the reaction of DL-bromosuccinic acid with hydrazine. The compound strongly inhibited aspartate aminotransferase and gave 50% inhibition at 1.3 microM when added simultaneously with L-aspartate to an assay mixture containing enzyme. Incubation of the enzyme with the compound prior to assay resulted in a much
R H, Yamada, Y, Wakabayashi, A, Iwashima, T, Hasegawa   +3 more
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Essential arginyl residues in aspartate aminotransferases

Biochemical and Biophysical Research Communications, 1975
Summary The active sites of the aspartate aminotransferases from both pig heart supernate and beef kidney mitochondria contain functional arginyl residues. Inactivation with butanedione in the presence of borate buffer, its reversal by gel filtration and irreversible inactivation with phenylglyoxal provide strong evidence for a functional role of ...
J F, Riordan, R, Scandurra
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Metabolic engineering of Escherichia coli for production of L-aspartate and its derivative β-alanine with high stoichiometric yield.

Metabolic Engineering, 2019
L-aspartate is an important 4-carbon platform compound that can be used as the precursor of numerous chemical products. The bioproduction of L-aspartate directly from biomass resources is expected to provide a more cost-competitive technique route.
X. Piao, Lei Wang, Baixue Lin, Hao Chen, Weifeng Liu, Y. Tao   +5 more
semanticscholar   +1 more source

A case of aspartate aminotransferase macroenzyme

Annals of Clinical Biochemistry: International Journal of Laboratory Medicine, 2008
Aspartate aminotransferase (AST) macroenzyme can result in elevated AST activity in patients with no disease. This case report describes a six-year-old boy who presented to his family doctor with a history of chronic constipation and lower back pain.
J, Cabrera-Abreu, R, Jain, P, Robinson, S, Edees, T, Staughton   +4 more
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[Aspartate aminotransferase].

Nihon rinsho. Japanese journal of clinical medicine, 1995
The characteristics and clinical usefulness for aspartate aminotransferase (AST) isoenzyme including apo- and holo-type enzymes were reviewed. The activation effect on mitochondrial- and cytosolic-AST (mAST and cAST) was compared in the presence of PALP, to sera of various diseases such non-alcoholic liver-, heart-, renal, and alcoholic liver diseases.
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Domain closure in mitochondrial aspartate aminotransferase

Journal of Molecular Biology, 1992
The subunits of the dimeric enzyme aspartate aminotransferase have two domains: one large and one small. The active site lies in a cavity that is close to both the subunit interface and the interface between the two domains. On binding the substrate the domains close together.
C A, McPhalen, M G, Vincent, D, Picot, J N, Jansonius, A M, Lesk, C, Chothia   +5 more
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Strain and catalysis in aspartate aminotransferase

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003
The notion of "ground-state destabilization" has been well documented in enzymology. It is the unfavourable interaction (strain) in the enzyme-substrate complex, and increases the k(cat) value without changing the k(cat)/K(m) value. During the course of the investigation on the reaction mechanism of aspartate aminotransferase (AAT), we found another ...
Hideyuki, Hayashi, Hiroyuki, Mizuguchi, Ikuko, Miyahara, Mohammad Mainul, Islam, Hiroko, Ikushiro, Yoshitaka, Nakajima, Ken, Hirotsu, Hiroyuki, Kagamiyama   +7 more
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Aminotransferases in Grapes. Isolation and Characterization of Aspartate Aminotransferase

American Journal of Enology and Viticulture, 1991
International ...
Sauvage, F.X., Romieu, C.G., Flanzy, C., Robin, J.P.   +3 more
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