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Prediction of non-intuitive metabolic targets with bayesian metabolic control analysis to improve 3-hydroxypropionic acid production in <i>Aspergillus niger</i>. [PDF]

open access: yesFront Bioeng Biotechnol
Dai Z   +13 more
europepmc   +1 more source

The Prognostic Role of Inflammation on Hepatocellular Carcinoma. [PDF]

open access: yesCancer Diagn Progn
Bilgetekin I   +8 more
europepmc   +1 more source
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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.
J, Tharakan, A, Hossenbocus, M J, Arthur
openaire   +2 more sources

Engineering aspartate transcarbamylase

Biochimie, 1990
Aspartate transcarbamylase from Escherichia coli is one of the most extensively studied regulatory enzymes as a model of cooperativity and allostery. Numerous methods are used to engineer variants of this molecule: random and site-directed mutagenesis, dissociation and reassociation of the catalytic and regulatory subunits and chains, construction of ...
G, Hervé   +4 more
openaire   +2 more sources

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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The aspartic proteases

Scandinavian Journal of Clinical and Laboratory Investigation, 1992
The Aspartic proteases (EC 3.4.23) are a group of proteolytic enzymes that share the same catalytic apparatus. Members of the aspartic protease family can be found in different organisms, ranging from humans to plants and retroviruses. The best known sources of aspartic proteases are the stomach of mammals, yeast and fungi, with porcine pepsin as the ...
openaire   +2 more sources

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