Wheat activity

Foods high ia sucrose, proteia, or starch (qv) tend to biad water less firmly and must be dried to a low moisture content to obtain microbial StabiHty. For example, grain and wheat flour can support mold growth at moisture contents above 15% (wet basis) and thus are stored at moisture contents below 14%. Stored grains and oil seeds must be kept at a water activity below 0.65 because certain molds can release aflatoxias as they grow. Aflatoxins are potent carciaogens (see Food toxicants, naturally occurring). 

Fig. 15. En2ymatic hydrolysis of wheat gluten at 72.5°C and pH 7.5 by an alkaline protease from Bacillus licheniformis. The numbers on the curves are en2yme—substrate ratios (E/S) in activity units (AU)/kg of protein where S = 7.4% (N x 5.7).

EC 3.4.24.3]. Purified by using /V-ethylmaleimide to activate the enzyme, and wheat germ agglutinin-agarose affinity chromatography [Callaway et al. Biochemistry 25 4757 1986],... 

A different mechanism operates in the wheat germ enzyme. 2,3-Bisphosphoglycerate is not a cofactor. Instead, the enzyme carries out intra-molecular phosphoryl group transfer (Figure 19.25). The C-3 phosphate is transferred to an active-site residue and then to the C-2 position of the original substrate molecule to form the product, 2-phosphoglycerate. 

Mg2+ 21 g 0.35 g Activates enzymes for body processes Chocolate, nuts, instant coffee, wheat bran... 

Miyamoto et al. (101) obtained four fractions from the seed coats of wheat which inhibited development of the wheat embryo. A component from one of the fractions responsible for 20% of the total inhibitor activity was crystallized but not identified. 

After this, we demonstrated the ability of wheat anionic POs to bind to the chitin of the cell walls of fungal pathogens. We called these POs "chitin-binding POs" (Maksimov et al., 2003). We were the first to demonstrate the binding of the anionic PO of wheat root to chitin (Maksimov et al., 1994). Besides this, we observed that in some species the activity of POs was increased in the unbound Armoracia rustkana, Lagenaria siceraria) or eluted Pisum sativum, Galega orientalis, Brassica oleraceae) fractions of proteins after interaction with chitin. 

We observed the activation of chitin-specific PO during infection with the causative agents of a number of diseases in wheat under the influence of Btpolaris soroktntana and the elicitors (Fig. 4), Septoria nodorum (Yusupova et al, 2006) and Tilletia caries (Khairullin et al., 2000) in potato infected by Phytophthora infestans (Maksimov et al., 2011), and in Aegilops umbellulata infected by Septoria nodorum (Maksimov et al, 2006). 

Yusupova Z.R. Akhmetova I.E. Khairullin R.M. Maksimov I.V. (2005) The effect of chitooligosaccharides on hydrogen peroxide production and anionic peroxidase activity in wheat coleoptiles / / Rus. J. of Plant Physiol. V. 52. P. 209-212. 

Mayoral, M.L., Atsmon, D., Gromet-Elhanan, Z. Shimshi, D. (1981). Effect of water stress on enzyme activities in wheat and related wild species Carboxylase activity, electron transport and photophosphorylation in isolated chloroplasts. Australian Jourrml of Plant Physiology, 8, 385-94. 

Blum, A., Mayer, J. Golan, G. (19886). The effect of grain number per ear (sink size) on source activity and its water-relations in wheat. Journal of Experimental Botany, 39, 106-114. 

Enhancement of the catalytic activity of the wheat germ, cell-free, protein synthesis system using a fortified translation extract... 

A wheat germ, cell-free, translation extract was fractionated into three concentrated parts using ammonium sulfate the 0 - 40 % saturated fraction, the 40 - 60 % saturated fraction, and the ribosome fraction. These fractions were tested for their ability to enhance the translational activity of the wheat germ, cell-free extract for dihydrofolate reductase. The fortified cell-free system supplemented with the 0 - 40 % ammonium sulfate fraction enhanced the efficiency of protein synthesis by 50 %. 

Previously, it has been reported that the amounts of eukaryotic initiation factors in wheat germ extract prepared by a common method were deficient for the translation of some kinds of mRNAs including a-amylase mRNA and (i-globin mRNA [2]. Therefore, it can be expected that the activity of wheat germ extract prepared by a common method can be enhanced by the simple addition of extract containing deficient initiation factors. In this study, a wheat germ extract was further purified partially by ammonium sulfate fractionation... 

The catalytic activities of the fortified wheat germ cell-free systems supplemented with each fraction were investigated (Fig. 2). As shown in Fig. 2, only 0 - 40 % ammonium sulfate fraction showed an enhancement in DHFR protein synthesis. This enhancement of protein experimental results and the fact that the various eukaryotic initiation factors are contained in synthesis was also confirmed by SDS-PAGE and autoradiography (Fig. 3). From the above 0-40 % ammonium sulfate fraction [5, 6], it can be concluded that the amount of initiation factors in a conventionally prepared wheat germ cell-fi extract is deficient for the translation of DHFR with internal ribosome entry site. Therefore, it needs to supplement a wheat germ cell-free extract with the fraction containing the limited initiation factors for the efficient protein translation, and this fortified cell-free system can be easily made by simple... 

The crystal structure of the HNL isolated from S. bicolor (SbHNL) was determined in a complex with the inhibitor benzoic acid." The folding pattern of SbHNL is similar to that of wheat serine carboxypeptidase (CP-WII)" and alcohol dehydrogenase." A unique two-amino acid deletion in SbHNL, however, is forcing the putative active site residues away from the hydrolase binding site toward a small hydrophobic cleft, thereby defining a completely different active site architecture where the triad of a carboxypeptidase is missing. 

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