• 제목/요약/키워드: K^+\

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REMARKS ON DIGITAL HOMOTOPY EQUIVALENCE

  • Han, Sang-Eon
    • 호남수학학술지
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    • 제29권1호
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    • pp.101-118
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    • 2007
  • The notions of digital k-homotopy equivalence and digital ($k_0,k_1$)-homotopy equivalence were developed in [13, 16]. By the use of the digital k-homotopy equivalence, we can investigate digital k-homotopy equivalent properties of Cartesian products constructed by the minimal simple closed 4- and 8-curves in $\mathbf{Z}^2$.

Status of Coated Conductor Development

  • Park, C.;Ko, R.K.;Song, K.J.;Chung, J.K.;Shi, D.Q.;Shin, K.C.;Youm, D.J.;Yoo, S.I.
    • 한국초전도학회:학술대회논문집
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    • 한국초전도학회 2003년도 High Temperature Superconductivity Vol.XIII
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    • pp.6-6
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    • 2003
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GREEN'S ADDITIVE COMPLEMENT PROBLEM FOR k-TH POWERS

  • Ding, Yuchen;Wang, Li-Yuan
    • 대한수학회지
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    • 제59권2호
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    • pp.299-309
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    • 2022
  • Let k ⩾ 2 be an integer, Sk = {1k, 2k, 3k, …} and B = {b1, b2, b3, …} be an additive complement of Sk, which means all sufficiently large integers can be written as the sum of an element of Sk and an element of B. In this paper we prove that $${{\lim}\;{\sup}}\limits_{n{\rightarrow}{\infty}}\;{\frac{{\Gamma}(2-{\frac{1}{k}})^{\frac{k}{k-1}}{\Gamma}(1+{\frac{1}{k}})^{\frac{k}{k-1}}n^{\frac{k}{k-1}}-b_n}{n}}\;{\geqslant}\;{\frac{k}{2(k-1)}}\;{\frac{{\Gamma}(2-{\frac{1}{k}})^2}{{\Gamma}(2-{\frac{2}{k}})}},$$ where 𝚪(·) is Euler's Gamma function.

에리스로마이신 고도내성 대장균 209K 유래 마크로라이드-포스포트란스페라제 K의 정제 및 특성 (The Purfication and Characterization of Macrolide-Phosphotransferase K of Escherichia coli 209K Highly Resistant to Erythromycin)

  • 김숙경;오태권;백문창;홍종수;김병각;최응칠
    • 약학회지
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    • 제41권3호
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    • pp.359-364
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    • 1997
  • Resistance gene mphK was cloned from Escherichia coli 209K strain which is highly resistant to erythromycin (EM). By using the cloned plasmid pGE64, E. coli NM522 was transformed. The comparison of macrolide-phosphotransferase K [MPH(K)] activity between E. coli 209K and E. coli NM522(pGE64) showed that the total enzyme activity of MN522(pGE64) was fifty-fole higher than that of 209K. To identify characteristics of MPH(K) more precisely. MPH(K) was isolated and purified from the NM522 (pGE64). The final purification f MPH(K) through several stages of purification process was 89 fole and the overall recovery was 11%. This enzyme was monomer with the molecular weight of 34 kDa and its isoelectric point (pI) was 5.0. The optimal pH and temperature for activity were 8.0 and $40^{\circ}C$, respectively.

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