- 영문명
- Characteristics of superoxide dismutases of mulberry leaf
- 발행기관
- 한국육종학회
- 저자명
- 윤성중(Song Joong Yun) 이완주(Won Chu Lee)
- 간행물 정보
- 『한국육종학회지』Vol.26 No.4, 389~393쪽, 전체 5쪽
- 주제분류
- 농수해양 > 기타농수해양
- 파일형태
- 발행일자
- 1994.12.30

국문 초록
영문 초록
Superoxide dismutases(SODs), the first enzyme involved in the protective mechanism from the deleterious superoxide radicals, converts superoxides to H₂O₂. Some characteristics of mulberry SODs were examined by the nitro bule tetrazolium reduction method. Mulberry leaves contained three or four major SODs depending on the varieties. It was found by the inhibitor test that mulberry leaf contained two Cu/ZnSODs and one or two FeSODs and no MnSOD. This finding of FeSOD in mulberry leaf made mulberry a member of the rare FeSOD containing plant species. There were no varietal differences in the Cu/ZnSOD isozyme patterns. FeSODs, however, showed different varietal isozyme patterns by the different combinations of the two FeSOD isozymes. Relatively large differences in the levels of SOD activity were detected in the mulberry varieties. It was interesting that Yongchonppong which has the highest level of cold-hardiness showed the highest SOD activity among the varieties tested.
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