Results 211 to 220 of about 200,089 (263)

Aspartate aminotransferase isoenzymes

Clinical Biochemistry, 1990
Aspartate aminotransferase (AST, EC 2.6.1.1) exists in human tissues as two distinct isoenzymes, one located in the cytoplasm (c-AST), and the other in mitochondria (m-AST). Striated muscle, myocardium, and liver tissues are the main sources of AST. A growing body of information suggests that determination of AST isoenzymes in human serum is useful in ...
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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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Aspartate aminotransferase ofLactobacillus murinus

Folia Microbiologica, 1988
Aspartate aminotransferase from Lactobacillus murinus is thermostable, its activity being not changed for two months at temperatures between 4 and -70 degrees C. Maximum activity was observed at 40 degrees C and pH 7.3 in phosphate buffer (30 mmol/L). delta G* Value of 26.3 kJ/mol was calculated from the Arrhenius plot.
G, Rollan, M C, Manca de Nadra, A, Pesce de Ruiz Holgado, G, Oliver   +3 more
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Immobilization of aspartate aminotransferase on agarose

Biochimie, 1989
Various methods for immobilization of aspartate aminotransferase (AspAT; from cytosolic fraction of pig heart) on agarose were tested. Aldehyde-, thiol-, and CNBr-activated agaroses were studied in detail. The capacity of the aldehyde support to firmly bind protein was less than 0.2 mg/ml, whereas the apparent remaining specific activity of the bound ...
K, Kurkijärvi, T, Korpela
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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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Determination of mitochondrial aspartate aminotransferase in serum

Clinica Chimica Acta, 1986
Two specific and sensitive immunoassay methods for the determination of mitochondrial aspartate aminotransferase (m-AST) are described. One is a sandwich enzyme immunoassay which measures immunologically active m-AST using polystyrene balls coated with anti-m-AST antibody and peroxidase-labelled anti-m-AST antibody as the second antibody. The detection
K, Hirano, K, Matsuda, T, Adachi, Y, Ito, K, Hayashi, F, Okuno, Y, Muto   +6 more
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Aspartate aminotransferase in the brain of the developing rat

Life Sciences, 1965
Abstract The biochemical immaturity of the rat brain at birth has been largely investigated in recent years (see for references, Sperry, 1955, 1962; Himwich, 1962). It has been tempting to relate neurochemical data to older findings on the physiological maturation of the organ.
G, Amore, V, Bonavita
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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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Aspartate aminotransferase: Investigation of the active sites

Journal of Molecular Graphics, 1990
An investigation of the crystal structure of cytosolic pig-heart aspartate aminotransferase (AAT, E.C.2.6.1.1) was carried out to determine the structural requirements for ligand recognition by the active site. Structural differences were observed between the two active sites of the AAT dimer.
T L, Nero, M G, Wong, S W, Oliver, M N, Iskander, P R, Andrews   +4 more
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The binding of bromophenol blue to aspartate aminotransferase

Archives of Biochemistry and Biophysics, 1976
Abstract Several experiments are presented that suggest that the sulfonphthalein dye, bromophenol blue, binds at, or near to, the active site of pig heart extramitochondrial aspartate aminotransferase (EC 2.6.1.1.). The binding is characterized at pH 8.0 by a bathochromic shift in the dye's visible spectrum from 590 to 599 nm.
R C, Harruff, W T, Jenkins
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