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'Cucumber Cotyledons' in keywords
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1992 (1)
1989 (1)
1Author    KenjiM. Atsui, Hiroyuki Shinta, H. Irom, Itsu Toyota, Tadahiko Kajiwara, AkikazuH. AtanakaRequires cookie*
 Title    Comparison of the Substrate Specificities of Lipoxygenases Purified from Soybean Seed, Wheat Seed, and Cucumber Cotyledons  
 Abstract    Lipoxygenases were highly purified from soybean seed, wheat seed and cucumber cotyle­ dons. Substrate specificities o f these lipoxygenases were studied by using an entire series o f (co6Z ,co9Z)-C 13~C24-dienoic acids as synthetic substrate analogues. Soybean lipoxygenase-1 and cucumber lipoxygenase showed broad specificities for these substrates while wheat lipoxygenase showed narrow specificities. Position o f dioxygenation to each substrate was an­ alyzed by high performance liquid chromatography. W ith soybean lipoxygenase-1 elongation o f the distance between the terminal carboxyl group and the site o f hydrogen removal in a substrate decreased the positional specificity o f dioxygenation, while, with cucumber lipoxy­ genase, shortening the distance decreased the specificity. It was suggested that cucumber lipoxygenase and soybean lipoxygenase-1 recognized the terminal carboxyl group o f a sub­ strate to arrange it only in one orientation at the reaction center. In case o f wheat lipoxygen­ ase, recognition o f the carboxyl group was thought to have crucial and essential role to secure the activity. 
  Reference    Z. Naturforsch. 47c, 85—8 (1992); received M ay 8/A ugust 27 1991 
  Published    1992 
  Keywords    Lipoxygenase, Cucumber Cotyledons, Soybean Seed, W heat Seed, Substrate Specificity 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0085.pdf 
 Identifier    ZNC-1992-47c-0085 
 Volume    47 
2Author    Kenji Matsui, Yasushi Shibata, Tadahiko Kajiwara, AkikazuH. AtanakaRequires cookie*
 Title    Separation of 13-and 9-Hydroperoxide Lyase Activities in Cotyledons of Cucumber Seedlings  
 Abstract    In cucumber cotyledons, both C6-and C9-aldehyde were formed via hydroperoxide (H PO) lyase activity. Because it has not been elucidated whether these activities are attri­ buted to one enzym e which can cleave both 13-and 9-H PO or to two or more enzym es each o f which specifically cleaves 13-or 9-H PO , an attempt to separate HPO lyase activity was done. Ion exchange chromatography separated this activity into two fractions, one o f which specifically cleaved 13-hydroperoxylinoleic acid and the other specifi­ cally cleaved the 9-isomer. 13-H PO -specific activity was most active at pH 8.0 and 9-H PO -specific one was at pH 6.5. SH -reagents inhibited both the lyases but to differ­ ent extents. 
  Reference    Z. Naturforsch. 44c, 883—885 (1989); received April 251989 
  Published    1989 
  Keywords    Cucumber Cotyledons, Hydroperoxide Lyase, Fatty A cid 13-H ydroperoxide, Fatty Acid 9-H ydroperoxide, Short-Chain A ldehydes 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0883_n.pdf 
 Identifier    ZNC-1989-44c-0883_n 
 Volume    44