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'Hydroperoxide Lyase' in keywords
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1992 (2)
1989 (1)
1Author    A. Kikazu, H. Atanaka, Tadahiko Kajiwara, KenjiM. Atsui, AkiraK. Itam UraRequires cookie*
 Title    Expression of Lipoxygenase and Hydroperoxide Lyase Activities in Tomato Fruits  
 Abstract    The distribution (or locarization) o f lipoxygenase (LOX) and hydroperoxide lyase (HPO lyase) activities in ripening and ripe tomato fruits was investigated. The highest LOX activity existed between skin and outer flesh o f tom ato fruits. HPO lyase showed no tissue specificity. LOX specifically formed linoleic acid 9-£',Z-hydroperoxide (9-.E,Z-HPO) from linoleic acid (LA), whereas HPO lyase specifically cleaved 13-Z.^-H PO . A lthough a low level (0.36 ± 0.069 nm ol/g fr. wt.) o f hexanal was detected in the intact tom ato fruit, HPOs were not detected. When a tom ato fruit was injured by cutting it into 8 fragments and incubated at 25 °C, hexanal increased to 1.642 nmol/g fr.wt. by 30 min. By hom ogenizing at pH 6.3, hex-anal increased to 21.1 nm ol/g fr.wt. during a 30 min incubation. U V irradiation o f tom ato fruits also increased the formation o f hexanal. From these results, LOX and HPO lyase are considered to exist as latent forms and to begin the expression o f the activity upon injury. 
  Reference    Z. Naturforsch. 47c, 369—3 (1992); received M ay 27 1991/March 4 1992 
  Published    1992 
  Keywords    H istological Localization, Hydroperoxide Lyase, Injury, Lipoxygenase, T om ato Fruit 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0369.pdf 
 Identifier    ZNC-1992-47c-0369 
 Volume    47 
2Author    AkikazuH. Atanaka, T. Adahiko Kajiwara, Kenji Matsui, Hiromitsu ToyotaRequires cookie*
 Title    Substrate Specificity of Tea Leaf Hydroperoxide Lyase  
 Abstract    Substrate specificity o f tea leaf fatty acid hydroperoxide lyase was systematically investigat­ ed using an entire series o f co6-(5)-hydroperoxy-C14-C24 dienoic and trienoic acids as sub­ strates. Unexpectedly, the hydroperoxides o f C22 but not natural substrates, i.e., those o f C 18, showed the highest reactivities for the lyase. The reactivities o f the hydroperoxides o f trienoic acids were always four to ten times higher than those o f the dienoic acids. 
  Reference    Z. Naturforsch. 47c, 677—6 (1992); received June 24/July 24 1992 
  Published    1992 
  Keywords    Aldehyde, Fatty Acid Hydroperoxide, Hydroperoxide Lyase, Substrate Specificity, Tea Leaf 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0677.pdf 
 Identifier    ZNC-1992-47c-0677 
 Volume    47 
3Author    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