Results 331 to 340 of about 414,727 (380)

Macromolecular aspartate aminotransferase

European Journal of Gastroenterology & Hepatology, 1998
Macroenzymes are serum enzymes that have a greater molecular mass than the corresponding enzyme normally found in serum (Klonoff. West J Med 1980; 133: 392-407). Serum AST (aspartate aminotransferase) has rarely been reported to complex with immunoglobulins, resulting in an elevation in serum AST activity.
Ahmed Hossenbocus, Joseph Tharakan, Michael J. P. Arthur   +2 more
openaire   +3 more sources

Buffers for the reconstitution of aspartate aminotransferase

Biochemical and Biophysical Research Communications, 1988
The cofactor activation of the apoenzyme of pig heart cytosolic aspartate aminotransferase was studied in various buffers. Cationic buffers are shown to allow maximal reconstitution in the pH range of 5.0 to 9.0. Anionic buffers made up of mono- and dicarboxylates are found to affect reconstitution in a pH-dependent manner.
Tuongvan T. Tran, Mark R. Barnes, Lance C. Foster, David J. Kearney, Bob In-yu Yang, Joseph L. Lambing   +5 more
openaire   +3 more sources

Evolutionary analysis of aspartate aminotransferases

Journal of Molecular Evolution, 1995
Aspartate aminotransferase isoenzymes are located in both the cytosol and organelles of eukaryotes, but all are encoded in the nuclear genome. In the work described here, a phylogenetic analysis was made of aspartate aminotransferases from plants, animals, yeast, and a number of bacteria.
Craig J. Marshall, Kevin J. F. Farnden, Paul H. S. Reynolds, Christopher S. Winefield   +3 more
openaire   +2 more sources

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
Ryo-Hei Yamada, Takeshi Hasegawa, Yasuo Wakabayashi, Akio Iwashima   +3 more
openaire   +3 more sources

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.
A. Pesce De Ruiz Holgado, G. Oliver, G. C. Rollán, M. C. Manca de Nadra   +3 more
openaire   +3 more sources

Loss of Life Expectancy by 10 Years or More From Elevated Aspartate Aminotransferase: Finding Aspartate Aminotransferase a Better Mortality Predictor for All-Cause and Liver-Related than Alanine Aminotransferase.

American Journal of Gastroenterology, 2019
OBJECTIVES Serum alanine aminotransferase (ALT) and aspartate aminotransferase (AST) are 2 commonly ordered liver function tests, and ALT has long been considered more liver-specific than AST. Between the 2, the one which is better in predicting liver or
Kunlin Xie, Chien-Hua Chen, S. Tsai, P. Lu, Hong Wu, Yong Zeng, Y. Ye, H. Tu, Christopher Wen, Maosheng Huang, Yajie Zhang, Jun-Han Lee, M. Tsai, C. Wen, Xifeng Wu   +14 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.
R Jain, T Staughton, J Cabrera-Abreu, S Edees, P Robinson   +4 more
openaire   +3 more sources

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 ...
Yoshitaka Nakajima, Hiroyuki Kagamiyama, Mohammad Mainul Islam, Ikuko Miyahara, Ken Hirotsu, Hiroyuki Mizuguchi, Hideyuki Hayashi, Hiroko Ikushiro   +7 more
openaire   +3 more sources

Measurement of Aminotransferases: Part 1. Aspartate Aminotransferase

CRC Critical Reviews in Clinical Laboratory Sciences, 1984
Aminotransferases are ubiquitous enzymes of mammalian cells and several are of important diagnostic use. The application of aspartate aminotransferase activity measurements in serum from individuals suffering from myocardial infarction brought about a new dimension in clinical laboratory testing in the 1950s.
Robert Rej, Leslie M. Shaw
openaire   +2 more sources