Results 121 to 130 of about 15,491 (147)
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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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Aminotransferases in Grapes. Isolation and Characterization of Aspartate Aminotransferase

American Journal of Enology and Viticulture, 1991
International ...
Sauvage, F.X.   +3 more
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Stability of aspartate aminotransferase and alanine aminotransferase activities.

The Journal of laboratory and clinical medicine, 1983
Because there are conflicting data regarding the effect of different temperatures and durations of storage on the stability of the activities of aspartate aminotransferase (AST) and alanine aminotransferase (ALT), a new study has been conducted to re-examine this important issue.
Hyman J. Zimmerman   +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.
W.Terry Jenkins, Richard C. Harruff
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Glycation of Aspartate Aminotransferase and Conformational Flexibility

Biochemical and Biophysical Research Communications, 2000
Glycation of proteins alters biological function and changes cellular processes. Our study investigated the conformational changes that accompany glycation using the cardiac aspartate aminotransferase (cAAT). We examined the effects of brief and prolonged exposure of cAAT to glyceraldehyde (Glyc) and ribose 5-phosphate (R5P).
Ines Seibel, Norbert W. Seidler
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The rotational relaxation time of aspartate aminotransferase

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1967
Abstract Two independent methods, sucrose density centrifugation and polarization of fluorescence, were used to study the molecular state of the enzyme aspartate amino-transferase at concentrations approaching those used in the enzymatic assays. 1. 1.
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Inhibition of coenzyme activation of aspartate aminotransferase

Biochemical and Biophysical Research Communications, 1983
Forty compounds were surveyed for their effect on the activation of pig heart apoaspartate aminotransferase by pyridoxamine 5'-phosphate. Most of the nucleotides, sugar phosphates, coenzymes, phospholipid precursors and inorganic oxyanions tested were found to be inhibitory.
Ashok K. Sawhney   +2 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
Yasutoshi Muto   +6 more
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Redesign of aspartate aminotransferase specificity to that of tyrosine aminotransferase

1994
The values of kcat/Km are strongly correlated with chain length for the reactions of E. coli tyrosine aminotransferase, but are nearly independent of this variable for aspartate aminotransferase. Both enzymes exhibit nearly equal reactivity with dicarboxylic acid substrates.
James J. Onuffer, Jack F. Kirsch
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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.
Giuseppe Amore, Vincenzo Bonavita
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