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韓學洙 現代醫學社 1968 現代醫學 Vol.9 No.4
The action of salt was studied to the anti-Klebsiella phage serum under the heating and ultra-'violet irradiation, with the following results. Salt protected the activity of antiserum from heat and ultraviolet ray. At the early stage of phage neutralization by the ultraviolet irradiated-antiserum, a delayed curve less than 2-hit curve On heating antiserum in salt solution, the serum protecting activities of salts were similar, so long as their cations were same. The anions showed no influence. On irradiating ultraviolet ray, the protecting action of salt was almost direct opposition to that !1"'*n heating. The anions showed major activity. 0.009 Mol of NaCl had no significant influence to the activity of antiserum. The mechanism of antibody protection of salt was discussed.
수분흡수에 따른 3,4'-ODA 폴리이미드 박막의 전기적 성질
한학수,조영일,서종철,오준석,이춘근 한국공업화학회 1998 응용화학 Vol.2 No.2
The object of this research is to measure the kinetics of water sorption and to explore the relationship between dielectric constant and water diffusion in chemically different polyimide thin films. Various backbone structure polyimides were synthesized from dianhydrides(PMDA, BTDA, BPDA 6FDA)and diamine(3,4'-ODA). For these four samples, dielectric properties as a function of time were measured as a function of time, by using a Film Dieleotric Property Analyzer(FDPA) in 100% R.H., and 25℃. The degree of dielectric variation by absorbing water varies from 0.64 to 0,86, and the dielectric variation coefficients(D_d) in films vary in the range of 1.6×10^(10)㎠/sec to 5.1 ×10^(10)㎠/sec. Also, degree of change in dielectric constants for the polyimide films by absorbing water is a nearly linear function of the amount of water uptake in spite of their difference of chemical structure.
各種 pH 및 加熱下에서 抽出한 菌體物質內의 蛋白質量에 對하여
韓學洙 現代醫學社 1968 現代醫學 Vol.9 No.4
The protein contents were measured of bacterial substance extracted under various pH and heat, with following results. The kinds of suspending fluid did not have any "influence for the results. Optimal condition for protein detection was neutral pH and temperature of 100C.