In the case of the oat seed proteins, no information can be obtained on pseudogenes such as has been reported for an oat globulin, nor can it Reversine structure detect genes expressed at such low levels that no EST contigs can be assembled. Neither case affects the major spectrum of ESTs representing mRNAs available for polypeptide synthesis or has any functional implication for the spectrum of avenin and globulin proteins in oat seeds. A comparison of oat cultivars for immunogenicity for patients with celiac disease found a range of reactivity. Such studies offer the opportunity to associated celiac reactivity with specific sets of seed proteins. The increasing efficiency of DNA sequencing could be used to perform deep ESTs on oat seed from such sets of germplasms. If specific sequences and epitopes could be associated with levels of celiac response, the ESTs could serve as a complement or substitute for immunological or clinical initial evaluations of oat cultivars. In this study, TfdEI and TfdEII display moderate stability at mesophilic temperatures and in the presence of various compounds such as detergents, organic solvents, along with urea which normally affects the enzyme structure. TfdEI and TfdEII showed high stability against Tween 80 and TritonX-100. TfdEII exhibited higher residual activity in the presence of 5% Tween 80 as compared to 1% Tween 80. This may be attributed to higher stability of the enzyme in the presence of 5% Tween 80 as compared to 1% Tween 80 as many studies have reported Tween 80 to increase enzyme stability and yield of proteins The other dienelactone hydrolase from this class of enzymes are not reported to show stability against denaturing agents except a thermostable DLH from thermophilic archaea Sulfolobus solfataricus PI which has shown high thermostability and stability against denaturing agents. The stabilities of TfdEI and TfdEII against general protein-denaturing compounds such as SDS and urea obtained in this study indicate that strong hydrophobic interactions make up the stable core of these enzymes and that the enzymes may have a high surface hydrophobicity, which are attractive properties for their possible industrial and biochemical applications. Our study confirms a number of prior reports of HIV-1-specific IgA in the genital tracts of HIV-1-exposed seronegative women. Between 38% and 82% of highly exposed seronegative women have been reported to have genital HIV-1-specific IgA, although one study of uninfected sex workers from the Gambia failed to detect any vaginal antibody responses against HIV-1. In our study, 9/57 women had vaginal HIV-1-specific IgA antibodies. Reasons for divergent frequencies in different studies and cohorts have been discussed elsewhere, but actual exposure rates to HIV-1 should be a major determinant. It is not surprising that IgA frequencies in our cohort were at the lower end of the reported range, because HPTN 035 study subjects, including the 57 women we studied, were not screened for self-reported risk factors such as frequent unprotected sex, a known HIV-infected partner and/or commercial sex work.