In this study, these RILs were used to analyze the role of pullulanase and SSIII on kernel modification. We found that the activity of pullulanase-type starch debranching enzyme was positively correlated with the kernel vitreousness and SSIII may influence pullulanase to affect starch structure and properties. Therefore, we propose that pullulanase and SSIII could play an important role in promoting formation of vitreous endosperm by altering the fine structure of starch. High mobility group box 1 was first discovered in calfthymi as a nuclear protein that contained a unique DNA-binding domain and Pyrimethamine showed rapid migration in polyacrylamide gels, a property of the HMG superfamily. The two HMG-box containing HMGB proteins are only present in multicellular animals, and the HMGB gene apparently arose through the fusion of two different genes, each coding for one of the boxes. Mammalian HMGB1 encodes 219 amino acids and contains two DNA-binding motifs that are arranged in tandem, following a long negatively charged C-terminus that is rich in aspartic and glutamic acids, which differ in length or are absent. By contrast, yeast HMGBs have only one HMG box domain and no acidic tail. HMG proteins can bind to cruciform, double- and single-stranded DNA with high affinity through HMG-box and acidic C-terminus. Interactions between DNA and HMGs are mediated by basic amino acid residues of the protein. Structural studies using nuclear magnetic resonance spectroscopy established that the DNA binding domain of HMG has an L-shaped structure made of three a-helices that provide surfaces for potential interactions with both DNA and protein. In higher organisms, HMGBs are ubiquitously expressed in cell nuclei and act as DNA chaperones that influence multiple processes in chromatin, such as transcription, replication, recombination, DNA repair and genomic stability. Variety of posttranslational modifications such as acetylation, Pitavastatin Calcium phosphorylation and methylation to HMGB can modulate not only HMGB1 protein function but also its subcellular location and eventual secretion. HMGB1 is a prototypical damage associated molecular pattern and the only one of these proteins that can be passively and actively secreted into the extracellular milieu, where it acts as cytokines, chemokines and growth factors that promotes cell migration and inflammation.