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A Model of Multiprocessor System with Communication Delays and Its Scheduling Method
Takashi Otsuka,Hironori Youhata,Qi-Wei Ge,Mitsuru Nakata,Yuu Moriyama,Hirotoshi Tonou 대한전자공학회 2008 ITC-CSCC :International Technical Conference on Ci Vol.2008 No.7
This paper aims at developing a scheduling method for multiprocessor systems with communication time. In this paper, we firstly propose a model of multiprocessor system with communication time occurring in reading data. Then, for the proposed model, we propose a scheduling method (called AMCN scheduling method) that (ⅰ) divides a task graph to subgraphs so that a task (called node hereafter) and its successors and predecessors are as much as possible included in the same subgraph to shorten communication time; and (ⅱ) uses a fixed processor to execute all the nodes of a subgraph. Finally, we do computational simulation experiments to evaluate our scheduling method.
Cloning of Agarase Gene from Non-Marine Agarolytic Bacterium Cellvibrio sp
( Ariga Osamu ),( Takayoshi Inoue ),( Hajime Kubo ),( Kimi Minami ),( Mitsuteru Nakamura ),( Michi Iwai ),( Hironori Moriyama ),( Mitsunori Yanagisawa ),( Kiyohiko Nakasaki ) 한국미생물 · 생명공학회 2012 Journal of microbiology and biotechnology Vol.22 No.9
Agarase genes of non-marine agarolytic bacterium Cellvibrio sp. were cloned into Escherichia coli and one of the genes obtained using HindIII was sequenced. From nucleotide and putative amino acid sequences (713 aa, molecular mass; 78,771 Da) of the gene, designated as agarase AgaA, the gene was found to have closest homology to the Saccharophagus degradans (formerly, Microbulbifer degradans) 2-40 aga86 gene, belonging to glycoside hydrolase family 86 (GH86). The putative protein appears to be a non-secreted protein because of the absence of a signal sequence. The recombinant protein was purified with anion exchange and gel filtration columns after ammonium sulfate precipitation and the molecular mass (79 kDa) determined by SDS-PAGE and subsequent enzymography agreed with the estimated value, suggesting that the enzyme is monomeric. The optimal pH and temperature for enzymatic hydrolysis of agarose were 6.5 and 42.5ºC, and the enzyme was stable under 40ºC. LC-MS and NMR analyses revealed production of a neoagarobiose and a neoagarotetraose with a small amount of a neoagarohexaose during hydrolysis of agarose, indicating that the enzyme is a β-agarase.