Results 221 to 230 of about 13,961 (264)
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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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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).
N W, Seidler, I, Seibel
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[The complex of aspartate aminotransferase with D-aspartate].

Biofizika, 1995
We report here the x-ray studies of the complex cytosolic aspartate aminotransferase from chicken heart with D-aspartate at 2,7 A resolution. Crystals of the complex was prepared by diffusing D-aspartate into free enzyme crystals; their space group is P 2(1)2(1)2(1) with cell dimensions (A): a = 62.59; b = 117.83; c = 124.38.
V M, Kochkina   +5 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.
openaire   +1 more source

A paediatric case of macro aspartate aminotransferase

Annals of Clinical Biochemistry: International Journal of Laboratory Medicine, 2008
Macroenzymes are enzymes in plasma that have a higher molecular mass than the corresponding enzyme normally present under (patho) physiological conditions. Macro species have been described for most routinely measured enzymes, but with only a few reports of macro species with aspartate aminotransferase (AST), and in particular very few reports in ...
Robert, Lord   +2 more
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Is Aspartate Aminotransferase Enough?

American Journal of Gastroenterology, 2000
GIANNINI, EDOARDO GIOVANNI   +1 more
openaire   +3 more sources

Structural Studies of Aspartate Aminotransferase Isozymes

1982
Enzymes which depend for their activity on the cofactor pyridoxal 5’-phosphate have been the object of extensive study over the last thirty or more years. One of the main reasons for this has been that the chemistry of the cofactor is well understood, and knowledge of the chemistry of the cofactor gives direct insights into the mechanisms of action of ...
D, Barra, F, Bossa, S, Doonan
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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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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.
Jack F. Kirsch, James J. Onuffer
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Primary structures of aspartate aminotransferases

Biochemical Society Transactions, 1984
F, Bossa, D, Barra, S, Doonan
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