Identification of a Group of Novel γ-Gliadin Genes

γ-Gliadins are an important component of wheat seed storage proteins. Four novel γ-gliadin genes （Gli-ngl to Gli-ng4） were cloned from wheat （Triticum aestivum） and Aegilops species. The novel γ-gliadins were much smaller in molecular size when compared to the typical γ-gliadins, which was caused by deletion of the non-repetitive domain, glutamine-rich region, 3＂ part of the repetitive domain, and 5＇ part of the C-terminal, possibly due to illegitimate recombination between the repetitive domain and the C-terminal. As a result, Gli-ngl and Gli-ng4 only contained two and three cysteine residues, respectively. Gli-ngl, as the representative of novel γ-gliadin genes, has been sub-cloned into an Escherichia coli expression system. SDS- PAGE indicated that the both cysteine residues of Gli-ngl could participate in the formation of intermolecular disulphide bonds in vitro. Successful cloning of Gli-ngl from seed cDNA of T. aestivum cv. Chinese Spring suggested that these novel γ-gliadin genes were normally transcribed during the development of seeds. Phylogenic analysis indicated that the four novel γ-gliadin genes had a closer relationship with those from the B （S） genome of wheat.

Simple and efficient method for synthesis of metallodeutero-porphyrin derivatives bearing symmetrical disulphide bond

A novel thiol-derivative porphyrin[2,7,12,18-tetramethyl-13,17-di（3-disulfidepropyl）porphyrin]bearing the symmetrical disulphide bond and its metal complexes have been successfully prepared by means of modification on naturally easily derived heme.The results are described by MS-MS and UV-vis spectroscopy.