Results 151 to 160 of about 10,082 (205)
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Insulin Aspart-szjj: An Insulin Aspart Biosimilar
Clinical Drug InvestigationInsulin aspart-szjj (MERILOG™) is a biosimilar of the reference rapid-acting insulin analog, insulin aspart, and is approved for the same indication as reference insulin aspart: to improve glycemic control in adult and pediatric patients with diabetes mellitus. The physicochemical characteristics of insulin aspart-szjj were similar to reference insulin
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Expert Opinion on Drug Metabolism & Toxicology, 2006
Insulin aspart, an analogue of human insulin, which is approved for use in people with diabetes, is more rapidly absorbed and achieves higher plasma concentrations than human soluble insulin following subcutaneous injection. Hence, it has a faster and more effective glucose-lowering action, with superior control of postprandial hyperglycaemia compared ...
David, Owens, Jiten, Vora
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Insulin aspart, an analogue of human insulin, which is approved for use in people with diabetes, is more rapidly absorbed and achieves higher plasma concentrations than human soluble insulin following subcutaneous injection. Hence, it has a faster and more effective glucose-lowering action, with superior control of postprandial hyperglycaemia compared ...
David, Owens, Jiten, Vora
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Aspartate as an Ergogenic Supplement
Sports Medicine, 2008Aspartate has been regularly listed in exercise physiology textbooks as an ergogenic substance since the first known trial by Professor Henri Laborit's laboratory in the late 1950s, aimed at verifying its ergogenic potential. The main outcomes of aspartate supplementation are attenuation of exercise-induced hyperammonaemia and increase of exercise ...
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[The complex of aspartate aminotransferase with D-aspartate].
Biofizika, 1995We 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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On aspartate transcarbamylase kinetics
Journal of Theoretical Biology, 1980Abstract We present direct calculations on aspartate transcarbamylase (ATCase) kinetics. New knowledge about ATCase quaternary structure are considered. “Decorated” Ising model is used for evaluating the statistical properties. Comparison with experimental data is considered. The theoretical results agree very well with experimental data.
E, Marchi, J, Horas
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Engineering aspartate transcarbamylase
Biochimie, 1990Aspartate 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
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Inhibition of glutamate-aspartate transaminase by β-methylene-DL-aspartate
Biochemical Pharmacology, 1983beta-Methylene-DL-aspartate, a new beta, gamma-unsaturated amino acid, is an irreversible inhibitor of soluble pig heart glutamate-aspartate transaminase (Ki approximately 3 mM with respect to the L-form; limiting rate constant for inactivation approximately 0.4 min-1).
A J, Cooper +4 more
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Aspartate aminotransferase isoenzymes
Clinical Biochemistry, 1990Aspartate 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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