• 제목/요약/키워드: Mori domain

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STRONG MORI MODULES OVER AN INTEGRAL DOMAIN

  • Chang, Gyu Whan
    • 대한수학회보
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    • 제50권6호
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    • pp.1905-1914
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    • 2013
  • Let D be an integral domain with quotient field K, M a torsion-free D-module, X an indeterminate, and $N_v=\{f{\in}D[X]|c(f)_v=D\}$. Let $q(M)=M{\otimes}_D\;K$ and $M_{w_D}$={$x{\in}q(M)|xJ{\subseteq}M$ for a nonzero finitely generated ideal J of D with $J_v$ = D}. In this paper, we show that $M_{w_D}=M[X]_{N_v}{\cap}q(M)$ and $(M[X])_{w_{D[X]}}{\cap}q(M)[X]=M_{w_D}[X]=M[X]_{N_v}{\cap}q(M)[X]$. Using these results, we prove that M is a strong Mori D-module if and only if M[X] is a strong Mori D[X]-module if and only if $M[X]_{N_v}$ is a Noetherian $D[X]_{N_v}$-module. This is a generalization of the fact that D is a strong Mori domain if and only if D[X] is a strong Mori domain if and only if $D[X]_{N_v}$ is a Noetherian domain.

The innate immune response transcription factor Bombyx mori Relish1 induces high-level antimicrobial peptides in silkworm

  • Kim, Seong-Wan;Kim, Seong-Ryul;Goo, Tae-Won;Choi, Kwang-Ho
    • International Journal of Industrial Entomology and Biomaterials
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    • 제37권2호
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    • pp.49-54
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    • 2018
  • To artificially enhance antimicrobial peptide expression in Bombyx mori, we constructed genetically engineered silkworms overexpressing Rel family transcription factor. The truncated BmRelish1 (BmRelish1t) gene contained a Rel homolog domain (RHD), nuclear localization signal (NLS), acidic and hydrophobic amino acid (AHAA)-rich region, and death domain (DD), but no ankyrin-repeat (ANK) domain. The BmRelish1t gene was controlled by B. mori cytoplasmic actin 3 promoter in the PiggyBac transposon vector. Chromosome analysis of G1 generations of a transgenic silkworm with EGFP expression confirmed stable insertion of BmRelish1t. BmRelish1t gene overexpression in transgenic silkworms resulted in higher mRNA expression levels of B. mori antimicrobial peptides such as lebocin(~20.5-fold), moricin(~8.7-fold), and nuecin(~17.4-fold) than those in normal silkworms.

ON v-MAROT MORI RINGS AND C-RINGS

  • Geroldinger, Alfred;Ramacher, Sebastian;Reinhart, Andreas
    • 대한수학회지
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    • 제52권1호
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    • pp.1-21
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    • 2015
  • C-domains are defined via class semigroups, and every C-domain is a Mori domain with nonzero conductor whose complete integral closure is a Krull domain with finite class group. In order to extend the concept of C-domains to rings with zero divisors, we study v-Marot rings as generalizations of ordinary Marot rings and investigate their theory of regular divisorial ideals. Based on this we establish a generalization of a result well-known for integral domains. Let R be a v-Marot Mori ring, $\hat{R}$ its complete integral closure, and suppose that the conductor f = (R : $\hat{R}$) is regular. If the residue class ring R/f and the class group C($\hat{R}$) are both finite, then R is a C-ring. Moreover, we study both v-Marot rings and C-rings under various ring extensions.

THE CLASS GROUP OF D*/U FOR D AN INTEGRAL DOMAIN AND U A GROUP OF UNITS OF D

  • Chang, Gyu Whan
    • Korean Journal of Mathematics
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    • 제17권2호
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    • pp.189-196
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    • 2009
  • Let D be an integral domain, and let U be a group of units of D. Let $D^*=D-\{0\}$ and ${\Gamma}=D^*/U$ be the commutative cancellative semigroup under aU+bU=abU. We prove that $Cl(D)=Cl({\Gamma})$ and that D is a PvMD (resp., GCD-domain, Mori domain, Krull domain, factorial domain) if and only if ${\Gamma}$ is a PvMS(resp., GCD-semigroup, Mori semigroup, Krull semigroup, factorial semigroup). Let U=U(D) be the group of units of D. We also show that if D is integrally closed, then $D[{\Gamma}]$, the semigroup ring of ${\Gamma}$ over D, is an integrally closed domain with $Cl(D[{\Gamma}])=Cl(D){\oplus}Cl(D)$; hence D is a PvMD (resp., GCD-domain, Krull domain, factorial domain) if and only if $D[{\Gamma}]$ is.

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EXTENSIONS OF NAGATA'S THEOREM

  • Hamed, Ahmed
    • 대한수학회지
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    • 제55권4호
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    • pp.797-808
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    • 2018
  • In [1], the authors generalize the concept of the class group of an integral domain $D(Cl_t(D))$ by introducing the notion of the S-class group of an integral domain where S is a multiplicative subset of D. The S-class group of D, $S-Cl_t(D)$, is the group of fractional t-invertible t-ideals of D under the t-multiplication modulo its subgroup of S-principal t-invertible t-ideals of D. In this paper we study when $S-Cl_t(D){\simeq}S-Cl_t(D_T)$, where T is a multiplicative subset generated by prime elements of D. We show that if D is a Mori domain, T a multiplicative subset generated by prime elements of D and S a multiplicative subset of D, then the natural homomorphism $S-Cl_t(D){\rightarrow}S-Cl_t(D_T)$ is an isomorphism. In particular, we give an S-version of Nagata's Theorem [13]: Let D be a Krull domain, T a multiplicative subset generated by prime elements of D and S another multiplicative subset of D. If $D_T$ is an S-factorial domain, then D is an S-factorial domain.

Detection of the expression of a Bombyx mori Atypical Protein Kinase C in BmPLV-Infected Larval Midgut

  • Cao, Jian;He, Yuanqing;Li, Guohui;Chen, Keping;Kong, Jie;Wang, Fenghua;Shi, Jing;Yao, Qin
    • International Journal of Industrial Entomology and Biomaterials
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    • 제22권2호
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    • pp.59-64
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    • 2011
  • Protein kinase C (PKC) is involved in many cellular signaling pathways, it participates in many physiological processes, such as cell cycle, growth, proliferation, differentiation and apoptosis. To investigate the effect of PKC on the silkworm midgut tissue infection of Bombyx mori parvo-like virus (BmPLV), a B. mori atypical protein kinase C (BmaPKC) gene was cloned from larval midgut tissue, expressed in E. coli and purified. Additionally, the BmPLV susceptible silkworm strain and resistant silkworm strain were used to test the effect of the B. mori infection on BmPLV. The result showed that BmaPKC encodes a predicted 586 amino acid protein, which contains a C-terminal kinase domain and an N-terminal regulatory domain. The maximum expression amount of the soluble (His)6-tagged fusion protein was detected after 0.8 mmol/L IPTG was added and cultured at $21^{\circ}C$. The (His) 6-tagged fusion protein revealed about 73 kDa molecular weight which confirmed by western blot and mass spectrography. Furthermore BmaPKC protein were detected at 0-72 h post-infection in BmPLVinfected larval midgut tissue, western blot showed that as time went on, the expression of BmaPKC increased gradually in susceptible strain, the expression quantity on 72 h is 5 times of 0 h. However, in resistant strain, the expression quantity is slightly lower than susceptible strain. But no significant change in resistant strain was observed as time went on. The available data suggest that BmaPKC may involve in the regulation of BmPLV proliferation.

THE STRONG MORI PROPERTY IN RINGS WITH ZERO DIVISORS

  • ZHOU, DECHUAN;WANG, FANGGUI
    • 대한수학회보
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    • 제52권4호
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    • pp.1285-1295
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    • 2015
  • An SM domain is an integral domain which satisfies the ascending chain condition on w-ideals. Then an SM domain also satisfies the descending chain condition on those chains of v-ideals whose intersection is not zero. In this paper, a study is begun to extend these properties to commutative rings with zero divisors. A $Q_0$-SM ring is defined to be a ring which satisfies the ascending chain condition on semiregular w-ideals and satisfies the descending chain condition on those chains of semiregular v-ideals whose intersection is semiregular. In this paper, some properties of $Q_0$-SM rings are discussed and examples are provided to show the difference between $Q_0$-SM rings and SM rings and the difference between $Q_0$-SM rings and $Q_0$-Mori rings.

Molecular Cloning of a cDNA Encoding Putative Calreticulin from the Silkworm, Bombyx mori

  • Kim, Seong-Ryul;Lee, Kwang-Sik;Kim, Iksoo;Kang, Seok-Woo;Nho, Si-Kab;Sohn, Hung-Dae;Jin, Byung-Rae
    • International Journal of Industrial Entomology and Biomaterials
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    • 제6권1호
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    • pp.93-97
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    • 2003
  • We describe here the cloning of a cDNA encoding putative calreticulin (CRT) from the silkworm, Bombyx mori. The CRT cDNA comprised of 1,194 bp encoding 398 amino acid residues. B. mori. CRT has a HDEL sequence at the end of the C-domain. The B. morl, CRT showed 88% protein sequence identity to the G. mellonella CRT, 71 % to A. aegypti CRT, and 63% to H. sapiens CRT, Phylogenetic analysis revealed that the deduced amino acid sequences of the B. mori CRT formed a highly inclusive subgroup with other insect CRTs. Northern blot analysis exhibited an expression of the B. mori CRT gene in the fat body, evidencing the fat body as a major site for CRT synthesis.

Genomic Organization of Heat Shock Protein Genes of Silkworm Bombyx mori

  • Velu, Dhanikachalam;Ponnuvel, Kangayam M.;Qadri, Sayed M. Hussaini
    • International Journal of Industrial Entomology and Biomaterials
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    • 제15권2호
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    • pp.123-130
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    • 2007
  • The Hsp 20.8 and Hsp 90 cDNA sequence retrieved from NCBI database and consists of 764 bp and 2582 bp lengths respectively. The corresponding cDNA homologus sequences were BLAST searched in Bombyx mori genomic DNA database and two genomic contigs viz., BAAB01120347 and AADK01011786 showed maximum homology. In B. mori Hsp 20.8 and Hsp 90 is encoded by single gene without intron. Specific primers were used to amplify the Hsp 20.8 gene and Hsp 90 variable region from genomic DNA by using the PCR. Obtained products were 216 bp in Hsp 20.8 and 437 bp in Hsp 90. There was no variation found in the six silkworm races PCR products size of contrasting response to thermal tolerance. The comparison of the sequenced nucleotide variations through multiple sequence alignment analysis of Hsp 90 variable region products of three races not showed any differences respect to their thermotolerance and formed the clusters among the voltinism. The comparison of aminoacid sequences of B. mori Hsps with dipteran and other insect taxa revealed high percentage of identity growing with phylogenetic relatedness of species. The conserved domains of B. mori Hsps predicted, in which the Hsp 20.8 possesses ${\alpha}-crystallin$ domain and Hsp 90 holds HATPase and Hsp 90 domains.