Understanding of the contribution of environmental and genetic factors on the chemical composition of different grains is a critical issue in the area of food safety of cereal products. Numerous studies have reported that asparagine can form acrylamide, a toxic and potentially carcinogenic precursor compound, during a Milliard reaction. Therefore, studying the environmental and genetic effects ...

Many prokaryotes lack a tRNA synthetase to attach asparagine to its cognate tRNA(Asn), and instead synthesize asparagine from tRNA(Asn)-bound aspartate. This conversion involves two enzymes: a nondiscriminating aspartyl-tRNA synthetase (ND-AspRS) that forms Asp-tRNA(Asn), and a heterotrimeric amidotransferase GatCAB that amidates Asp-tRNA(Asn) to form Asn-tRNA(Asn) for use in protein synthesis....

Short term (2-hour) incorporation of nitrogen from nitrate, glutamine, or asparagine was studied by supplying them as unlabeled ((14)N) tracers to growing pea (Pisum sativum L.) leaves, which were previously labeled with (15)N, and then following the elimination of (15)N from various amino components of the tissue. Most components had active and inactive pools. Ammonia produced from nitrate was...

Since the advent of paper chromatographic methods in 1944 (l), extracts of a great many plant species have been examined for the presence of amino acids. Aspartic acid and its amide asparagine have almost invariably been found. Recognition of the importance of these substances goes back to the earliest days of plant biochemistry. Vauquelin and Robiquet first isolated asparagine in 1806 (2) from...

L-asparaginase (L-asparagine amido hydrolase, E.C.3.5.1.1) is an extra cellular enzyme that has received considerable attention since it is used as an anticancer agent. L-asparaginase belongs to an amidase group that hydrolyses the amide bond in Lasparagine to aspartic acid and ammonia. The clinical action of this enzyme as an anti-carcinogenic is attributed to the reduction of L-asparagine; tu...

A new enzyme termed GA: 1.2, possessing approximately equal amounts of glutaminase and asparaginase activity, has antitumor activities against cancers other than leuke mia, thus enlarging the potential for cancer therapy by amino acid deprivation. When tested against the asparagine-dependent EARAD-1 leukemia in the presence of the láclatedehydrogenase-elevating virus (LDH-virus), striking tumo...

L-Asparaginase has been widely used for the treatment of acute lymphoblastic leukemia. Therapeutic and toxic effects in the central nervous system have been noted with systemic treatment. In order to better define the relationship between L-asparaginase administration and cerebrospinal fluid (CSF) asparagine levels, L-asparaginase and asparagine were measured in the CSF of rhesus monkeys follow...

Because of their low asparagine synthetase (ASNS) expression and asparagine biosynthesis, acute lymphoblastic leukemia (ALL) cells are exquisitely sensitive to asparagine depletion. Consequently, asparaginase is a major component of ALL therapy, but the mechanisms regulating the susceptibility of leukemic cells to this agent are unclear. In 288 children with ALL, cellular ASNS expression was mo...

The mobilization of stored carbohydrates (sucrose and starch) and proteins during sucrose starvation was studied with sycamore (Acer pseudoplatanus L.) cells. When almost all the intracellular carbohydrate pools had disappeared, the cell protein content declined progressively whereas asparagine determined by either (13)C nuclear magnetic resonance or reversed phase high performance liquid chrom...

The degradation of proteins by asparagine deamidation and aspartate isomerization is one of several chemical degradation pathways for recombinant antibodies. In this study, we have identified two solvent accessible degradation sites (light chain aspartate-56 and heavy chain aspartate-99/101) in the complementary-determining regions of a recombinant IgG1 antibody susceptible to isomerization und...