Results 321 to 330 of about 21,862 (343)

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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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, Kazuko Matsuda, Kazuyuki Hirano, Tetsuo Adachi, Kyozo Hayashi, Yoshimasa Ito, Fumitaka Okuno   +6 more
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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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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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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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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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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, Bob In-yu Yang, Gina M. Hartmeier   +2 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 ...
Roberto Scandurra, James F. Riordan
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Is Aspartate Aminotransferase Enough?

American Journal of Gastroenterology, 2000
GIANNINI, EDOARDO GIOVANNI, TESTA, ROBERTO   +1 more
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Aspartate aminotransferases like it hot

1994
A remarkable tendency towards thermophilicity and thermostability seems to be a general trend of aspartate aminotrasferases (AspAT). This was first discovered by Jenkins et al. (1959) who introduced a vigourous heating step into their purification protocol for pig heart cytosolic enzyme. AspATs from different microorganisms living in different habitats
Gennaro Marino, Giovanni Sannia, Leila Birolo   +2 more
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