Wheat germ

Wheat germ contains coenzyme Q10, which synthesizes ATP and stabilizes mitochondria. In 1977, Peter Mitchell received a Nobel Prize for work on coenzyme Q10 and energy transfer. Coenzyme Q10 protects against mitochondrial diseases. It is efficacious in heart diseases and is a neuroprotectant, and hence is effective in Parkinson s disease. 

The usual definition of a neuroprotectant is an agent that aims to prevent neuronal death by inhibiting one or more of the pathophysiological steps in the processes that follow injury to the central nervous system (CNS) or ischemia due to occlusion of an artery or hypoxia due to any cause. This definition has now been extended to include protection against neurodegeneration and neurotoxins. The extended definition includes interventions that slows or halts the progression of neuronal degeneration. 

Wheat germ is the embryo of wheat berry. It is a good source of coenzyme Q10, vitamin E, choline, most of the B vitamins, the minerals calcium, magnesium, phophorus, and several trace elements. This chapter provides information only on coenzyme Q10, which is useful in the treatment of the pleiotropic manifestation of the following diseases  

Pearson s syndrome with pancytopenia Brain Ataxia Stroke Seizures Dementia Migraine Eye 

Ophthalmoplegia Optic neuropathy Pigmentary retinal degeneration Cataract 

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Additional basic wheat products are wheat berry (kernel), bulgar, cracked wheat, wheat germ, bran, and commercial cereals. See Ref. 56 for more information on wheat science technology. 

Nicotinamide and nicotinic acid are prevalent in many common foodstuffs and are especially concentrated in brewer s yeast, wheat germ and fiver. 

Methylcytosine (964 X = O) was synthesized in 1901 and its isolation from hydrolyzates of tubercule bacilli was reported in 1925. However, this was later shown to be incorrect and only about 1950 was it isolated by hydrolysis of the deoxyribonucleotide fractions from thymus, wheat germ and other sources (50MI21302). Nucleotides and a nucleoside of 5-methylcytosine are known. 

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],... 

In a study of the effect of nutrition on reproduction in the rat in the 1920s, Herbert Evans and Katherine Bishop found that rats failed to reproduce on a diet of rancid lard, unless lettuce or whole wheat was added to the diet. The essential factor was traced to a vitamin in the wheat germ oil. Named vitamin E by Evans (using the next available letter following on the discovery of vita-... 

FIGURE 19.25 The phosphoglycerate mutase of wheat germ catalyzes an intramolecn-lar phosphoryl transfer. 

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. 

Yeast, Pseudomonas, liver, wheat germ Yeast Liver... 

Heart muscle, Laetobaeillus Pig heart, wheat germ Spinach... 

Some of the nutrients lost when the wheat germ and bran are discarded are returned to the flour by adding small amounts of vitamins and minerals. Among the nutrients most commonly added are niacin, thiamine, riboflavin, folic acid, iron, and calcium. 

Other organic raw materials P-Sitosterol Lanolin, wool wax, cotton seed, wheat germ oil... 

Disodium wheat germ amido MEA-sulfosuccinate DWMS... 

Recently, an interesting example of the enzymatic kinetic resolution of a-acetoxyamide 8 was demonstrated using native wheat germ lipase and immobilized lipase PS (AMANO) (Scheme 5.6). 

Wheat germ agglutinin Widely used in studies of surfaces of normal cells and cancer cells... 

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... 

Fig. 1. Reconstruction of the cell-free protein synthesizing system with the partially purified wheat germ extracts. Control normal wheat germ cell-free system, (I) 0 - 40 % ammonium sulfate fraction 3 pi, 40 - 60 % ammonium sulfate fraction 4 pi, and ribosome 3 pi were added to 25 pi reaction mixture, (II) 0-40 % ammonium sulfate fraction 4 pi, 40 - 60 % ammonium sulfate fraction 4 pi, and ribosome 1.5 pi were added to 25 pi reaction mixture.

Translation reaction mixture contained 20 % (v/v) wheat germ extract and the followings (final concentrations) 60 mM HEPES/KOH (pH 7.6), 1 mM ATP, 100 pM GTP, 300 pM spermidine, 2 mM magnesium acetate, 40 mM potassium acetate, 160 pM each... 

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