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KMID : 0903619950360060863
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Journal of the Korean Society for Horticultural Science
1995 Volume.36 No. 6 p.863 ~ p.869
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Peroxidase Activity in Callus , Plantlets , and Cormlets of Gladiolus
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Abstract
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The study was carried out to investigate the characteristics of peroxidase and protein in the ealli, plantlets, cormels, and cormlets of gladiolus cv. Topaz. Peroxidase activity measured by absorbance methods was high tat 436 ㎚ and 470 ㎚. Peroxidase activity of plantlets and cormlets was higher at 10,000 xg supernatant compared with other fractions. Activity was higher at calli among materials. There was more protein in calli than that of plantlets and cormlets. Peroxidase activity in the plantlets and cormlets was the highest at pH 5.0 - 6.0 and 50℃ - 60℃ temperature conditions. After the investigation of peroxidase activity to guaiacol substrate, peroxidase activity in terms of Vmax value (umoles/mim/㎎ proteins) was the highest in calli and was 455.2 in cormlets, 441.7 in plantlets, respectively. Vmax value was the lowest in the cormels. As the results of affinity test to guaiacol substrates, calli showed the low affinity (Km value =2.5 × 10^(-6) M), and cormlets showed the highest affinity (Km value = 7.2 × 10^(-6) M). The number of protein bands by SDS - PAGE electrophoresis were more in the calli and few in plantlets. The band located at near 66 KDa was the most obvious in all the tested materials. Cormlets contained abundant protein bands having less than a 14 KDa. Plantlets containd few bands having less than a 30 KDa.
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