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Çѱ¹½Ä¹°ÇÐȸ / v.35, no.3, 1992³â, pp.185-190
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°³¶Äá (Phaseolus vulgaris L.) Á¾ÀÚ¼º¼÷¿¡ µû¸¥ Áöº£·¼¸° ¼ö»êÈÈ¿¼Ò Ȱ¼ºÀÇ º¯È I. $GA_{20}À»;GA_1$À¸·Î º¯È¯½ÃŰ´Â $3{eta}-Hydroxylase$
( Changes in Gibberellin Hydroxylase Activity during Seed Maturation of Phaseolus vulgaris L. I. $3{eta}-Hydroxylase$ Converting $GA_{20};to;GA_1$ ) |
| Á¤»ó¼ö; Çѱ¹°úÇбâ¼ú¿¬±¸¼Ò À¯Àü°øÇבּ¸¼Ò ½Ä¹°¼¼Æ÷»ý¹°Çבּ¸½Ç;
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| °³¶ÄáÀÇ µÎ ǰÁ¾(Á¤»óÁ¾ÀÎ Kentucky Wonder¿Í ¿Ö¼ºÁ¾ÀÎ Masterpiece)ÀÇ ¹Ì¼º¼÷ Á¾ÀڷκÎÅÍ ºÎºÐ Á¤Á¦ÇÑ GA $3{eta}-¼ö»êÈÈ¿¼Ò¸¦$ »ç¿ëÇÏ¿© $[^3H]GA_{20}$À¸·ÎºÎÅÍ $GA_1$·ÎÀÇ È¿¼ÒȰ¼ºÀÇ º¯È¸¦ Á¶»çÇÏ¿´´Ù. µÎ ǰÁ¾ÀÇ Á¾ÀÚ¼º¼÷¿¡ µû¸¥ $3{eta}$ ¼ö»êÈÈ¿¼Ò Ȱ¼ºÀÇ º¯È¿Í °¾à¿¡´Â Â÷À̰¡ ¾ø¾ú´Ù. ±ØÈ÷ ¹Ì¼º¼÷ÇÑ Á¾ÀÚ¿¡¼ ´ÜÀ§ ´Ü¹éÁú´ç GA $3{eta}-¼ö»êÈÈ¿¼Ò$ Ȱ¼ºÀÌ °¡Àå ³ô¾Ò´Ù. ´ÜÀ§ Á¾ÀÚ´ç È¿¼ÒÀÇ ºñȰ¼ºÀº °³È ÈÄ 21ÀÏ ÀüÈÄ¿¡¼ ÃÖ´ëÄ¡¸¦ ³ªÅ¸³»¾úÀ¸¸ç, Á¾ÀÚ°¡ ´õ¿í ¼º¼÷ÇÔ¿¡ µû¶ó Ȱ¼ºÀº °¨¼ÒµÇ¾ú´Ù. µ¿ÀÏ·®ÀÇ $3{eta}-¼ö»êÈÈ¿¼Ò$ Ȱ¼ºÀ» »ç¿ëÇÏ¿© $[17-^{13}C,;^3H_2];GA_{20}$ÀÇ ´ë»ç¸¦ Á¶»çÇÑ °á°ú, GA_1,;GA_5,;GA_6$À¸·ÎÀÇ º¯È¯À²Àº Á¾ÀÚ»ýÀå´Ü°è¿¡ °ü°è ¾øÀÌ °ÅÀÇ ÀÏÁ¤ÇÏ¿´´Ù. $GA_5·ÎºÎÅÍ;GA_6$ÀÇ epoxidationÀº Á¤Á¦ÇÑ $3{eta}-¼ö»êÈÈ¿¼ÒºÐȹ¿¡$ ÀÌ·ç¾îÁ³À¸¸ç(Kobayashi et al., 1991), ÀÌ ¹ÝÀÀÀº $3{eta}-¼ö»êÈÈ¿¼ÒÀÇ$ ±âÁúµé¸¸¿¡ ÀÇÇØ ƯÀÌÀûÀ¸·Î ¾ïÁ¦µÇ¾ú´Ù. ÀÌ·¯ÇÑ °á°ú´Â °³¶Äá ¹Ì¼º¼÷Á¾ÀÚ¿¡¼ $GA_{20}ÀÇ;3{eta}-¼ö»êȹÝÀÀ°ú;GA_5$ÀÇ epoxidationÀº µ¿ÀÏ È¿¼Ò¿¡ ÀÇÇØ Ã˸ŵÊÀ» ½Ã»çÇÑ´Ù. |
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| Changes in activity of gibberellin $3{eta}-hydroxylase$ which converts $[^3H]GA_{20};to;GA_1$ were studied during seed maturation using partially purified enzyme preparations of two cultivars, Kentucky Wonder (normal) and Masterpiece (dwarf) of Phaseolus vulgaris. The specific activity of $3{eta}-hydroxylase$ per seed reached maximum at 21 days after flowering and subsequently decreased during seed maturation in both cultivars. The ratios of conversion of $[17-^{13}C,;^3H_2]GA_{20};to;GA_1.;GA_5,;and;GA_6$ by the same amount of $3{eta}-hydroxylase$ were almost identical. Epoxidation of $GA_5;to;GA_6$ is also catalyzed by the partially purified $3{eta}-hydroxylase$ preparation(Kobayashi et aI., 1991) and the conversion was inhibited by the substrates of $3{eta}-hydroxylase$. These results suggest that the same enzyme might catalyze $3{eta}-hydroxylase{;}of{;}GA_{20};to;GA_1$ and epoxidation of $GA_5;to;GA_6$.. |
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Journal of Plant Biology / v.35, no.3, 1992³â, pp.185-190
Çѱ¹½Ä¹°ÇÐȸ
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO199211920116054)
¾ð¾î : Çѱ¹¾î |
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| ³í¹® Á¦°ø : KISTI Çѱ¹°úÇбâ¼úÁ¤º¸¿¬±¸¿ø |
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