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Plasmonics - We investigate aluminum nanopatch/nanohole arrays surrounded by a dielectric material on plastic substrates for large area color printing. In this specific arrangement, metallic... 相似文献
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Yan-Hong He Guo-Gui Ning Ya-Lin Sun Yan Hu Xing-Yu Zhao Man-Zhu Bao 《Molecular breeding : new strategies in plant improvement》2010,26(1):19-29
A male sterile line was isolated in marigold (Tagetes erecta L.) and cytological analysis determined this to be a novel genic male sterility trait (Tems). Through the use of amplified fragment length polymorphisms (AFLPs) and bulked segregant analysis (BSA), tightly linked
markers of Tems were identified with a view towards a map-based cloning strategy. It was found that spontaneous homeotic conversion of floral
organs was the underlying cause of the male sterility in this marigold line. Thus, petals of male sterile plants resembled
sepal-like structures and the stamens were partially converted to styles, although without the full characteristics or function
of the true style organs. We have constructed a fine marker-based map for the Tems gene. This is intended to provide a tool for marker assisted selection (MAS) strategies in hybrid breeding and map-based
cloning strategies for the male sterility locus. We discuss the significance of this spontaneously derived genic male sterility
trait relating to the homeotic conversion of floral organs in marigold. 相似文献
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An endopeptidase (LEP-II), which has a unique substrate specificity, was purified to homogeneity by conventional chromatographic techniques from Streptococcus cremoris H61. The enzyme was a metalloendopeptidase since it was inhibited by EDTA and 1,10-phenanthroline; the metal-depleted enzyme could be fully reactivated by micromolar levels of Zn2+ and was not inhibited by specific inhibitors for serine or thiol protease. The molecular mass of the enzyme was estimated to be 80 kDa by Sephacryl S-300 gel filtration and high-performance liquid chromatography with a TSK-G3000SW column. The enzyme consisted of two identical subunits and the N-terminal sequence of LEP-II was determined up to the 19th residue. Although the enzyme had a broad substrate specificity it specifically hydrolyzed the peptide bonds involving the amino groups of hydrophobic amino acid residues. Various small polypeptides, such as alpha s1-CN(f1-23), alpha s1-CN(f91-100), oxidized insulin B chain, glucagon and some biologically active peptides were hydrolyzed. However, a variety of larger polypeptides or proteins, such as alpha s1-CN(f1-54), alpha s1-CN(f61-123), alpha s1-CN(f136-196), alpha s1-casein, beta-casein, and kappa-casein were not hydrolyzed. LEP-II recognized the size of its substrates, which were limited below a molecular mass of about 3.5 kDa. 相似文献