Immunoreaction indication, enzyme

Wheat starch is low in protein, ash and fiber, and contains no residual sulfites. Sulfur dioxide is detrimental to the viscoelastic character of wheat gluten and is not used in the commercial production of wheat starch.28,323 The protein content of ten samples of unmodified and modified wheat starches ranged from 0.06-0.22%.28 A 0.23% protein (0.0404% nitrogen) level in wheat starch essentially indicates a gluten-free starch, as confirmed by an enzyme immunoassay.324 That purity of wheat starch is important in diets for celiac individuals. Wheat starch-based, gluten-free flour products were not harmful in the treatment of celiac sprue and dermatitis herpetiformis,325 although traces of an immunoreactive gliadin can be found in wheat starch.326... 

An ADPGlc PPase cDNA clone, isolated from a maize endosperm library (Barton et al., 1986), hybridized with the small subunit cDNA clone from rice (Anderson etal., 1989). This maize ADPGlc PPase cDNA clone hybridizes to a transcript that is present in maize endosperm but absent in bt 2 endosperm. Thus, the bt 2 mutant appears to be the structural gene of the 55-kDa subunit of the ADPGlc PPase. These data also indicate that the nonphotosynthetic tissue ADPGlc PPase is also composed of two subunits and, on the basis of immunoreactivity, there is homology between the large and small subunits in the leaf enzyme with the subunits of a reserve tissue enzyme, respectively. 

The presence of the second active form of MIPS with a —65 kDa subunit indicated that the inositol requirement of the organism might be provided by the interplay of two different MIPS enzymes, probably by differential expression through time and space. The results indicate that the —65 kDa MIPS protein of Synechocystis might be coded by the ORF sill981, annotated as a putative acetolactate synthase (unpublished data from this laboratory). This gene also functionally complements the inositol auxotrophic yeast strain FY250 and Schizosaccharomyces pombe, a natural inositol auxotroph, and the expressed protein is immunoreactive to anti MIPS antibody. 

In summary, data available so far indicate that leaf and seed ADP-Glc PPases are heterotetramers composed of two different subunits, and that, on the basis of immunoreactivity and sequence data, there is corresponding homology between the subunits in the leaf enzyme and with the subunits of reserve tissue enzyme. 

NOS-positive neurones and activated neuroglial cells were the most prominent citruUine-positive structures (Keilhoff et al. 2000). Lack of citruUine-immunoreaction in neurones of nNOS knockout mice emphasised the dependency of cit-ruUine positivity on NOS activity, and likewise there was no citrulline staining after application of the NOS inhibitors 7-nitroindazole and l-N -(1-iminoethyl)lysine. The inhibition of argininosuc-cinate synthetase by a-methyl-DL-aspartate increased the number of citrulline-positive cells, apparently due to the reduction of the turnover rate of citrulline. Cells positive for NOS but negative for citrulline may indicate that the enzyme is either not activated or inhibited by cellular control mechanisms. The fact that not all citrulline-positive cells were NOS positive may be explained by an insufficient detection sensitivity or by disparate sites of citrulline production and recycling. 

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