• Title/Summary/Keyword: Pysiological Characterization

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Comparisons of Physiological Characteristics in Coriolus versicolor Intraspecific Strains (한국산 구름버섯의 균주간(菌株間) 생리적(生理的) 특성(特性) 비교(比較))

  • Park, Young-Do;Whang, Wan-Kyunn;Huh, Jae-Doo;Kim, Seong-Hwan;Park, Won-Mok
    • The Korean Journal of Mycology
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    • v.17 no.1
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    • pp.7-13
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    • 1989
  • This study was executed to investigate characterization of physiological genetic in Coriolus versicolor, basidiomycetes. The optimal media for mycelia culture were PDA, CVT-I and MES as solid media, 927 and CVT-III were good as liquid media, respectively. The optimal condition for mycelial culture was pH 5.6 and $25-30^{\circ}C$. Electrophoretic isozymes and protein patterns from mycelia identified very similar in 16001 and KD88001 strain, but the other species were very diffrent in band patterns. Especially, pattern of esterase seemed to be valuable tool as taxonomic techniques for indentifying species of Coriolus versicolor. Fruiting body was cultivated with artificial logs cultivation method; 16001 and KD88001 were very similar to fruiting body shapes and colours but 16001 and CVT-80 were different in their shapes, colours and making primordia. Therefore, 16001 and KD88001 were assumed to the same strain, but 16001, 16002 and CVT-80 had the different genetic background.

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Purification and Pysiological Characterization of Isoperoxidase from Oat Root Treated with Alachlor (Alachlor 처리후(處理後) 귀리 근단(根端)에 존재(存在)하는 동위과산화효소(同位過酸化酵素) 정제(精製) 및 효소(酵素)의 생리적(生理的) 특성(特性))

  • Kwon, S.W.;Han, K.S.;Kim, J.C.
    • Korean Journal of Weed Science
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    • v.14 no.1
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    • pp.56-61
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    • 1994
  • The cationic isoperoxidases were isolated from oat root tips which had been grown in treatment with $1{\times}10^{-4}$ M alachlor and purified about 30-fold by treatment with ethylalchol and ion exchange chromatography on DEAF-celluose and CM-sephadex medium. The oat root was found to contain three isoperoxidase. The major activity peak (B) represented 65% of the total isoperoxidase activity. After purification, the major peak of isoperoxidase was purified about 37-fold from the oat root. Analysis of the major peroxidase peak(column fraction 58-78) by SDS revealed a single band which corresponed to a molecular mass of 42.5 kD. In vitro, isoperoxidase activies were inhibited by IAA. Isoperoxidase(50 unit) significantly inhibited 70.2% of cell division in oat root and 54.2% of cell elongation in oat coleoptile as compared with control.

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