Endoplasmic reticulum as a site of phenylpropanoid and flavonoid metabolism in Hippeastrum
The nature of bound forms of enzymes of phenylpropanoid and flavonoid metabolism have been investigated in Hippeastrum CV Dutch Red Hybrid. Particulate compenents of petal homogenates were fractionated on sucrose gradients and the EDTA shift method was employed to characterize membranes of the endop...
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| Published in | Plant physiology (Bethesda) Vol. 74; no. 4; pp. 901 - 906 |
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| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
United States
American Society of Plant Physiologists
01.04.1984
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| Subjects | |
| Online Access | Get full text |
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| Abstract | The nature of bound forms of enzymes of phenylpropanoid and flavonoid metabolism have been investigated in Hippeastrum CV Dutch Red Hybrid. Particulate compenents of petal homogenates were fractionated on sucrose gradients and the EDTA shift method was employed to characterize membranes of the endoplasmic reticulum. In magnesium-containing gradients, a portion of phenylalanine ammonia lyase, chalcone synthase, glucosyl transferase, and all of the trans-cinnamate 4-monooxygenase and NADH Cytochrome c reductase (the last an endoplasmic reticulum marker) were associated with membranes equilibrating at 1.18 specific gravity. In gradients lacking magnesium and containing EDTA, the above activities--except chalcone synthase, which was lost--and protein were diminished at 1.18 specific gravity and enhanced at lower densities characteristic of membranes of the smooth endoplasmic reticulum. These results are consistent with the contention that endoplasmic reticulum is a site of phenylpropanoid and flavonoid metabolism in Hippeastrum. |
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| AbstractList | The nature of bound forms of enzymes of phenylpropanoid and flavonoid metabolism have been investigated in Hippeastrum CV Dutch Red Hybrid. Particulate components of petal homogenates were fractionated on sucrose gradients and the EDTA shift method was employed to characterize membranes of the endoplasmic reticulum. In magnesiumcontaining gradients, a portion of phenylalanine ammonia lyase, chalcone synthase, glucosyl transferase, and all of the trans-cinnamate 4-monooxygenase and NADH Cytochrome c reductase (the last an endoplasmic reticulum marker) were associated with membranes equilibrating at 1.18 specific gravity. In gradients lacking magnesium and containing EDTA, the above activities-except chalcone synthase, which was lost-and protein were diminished at 1.18 specific gravity and enhanced at lower densities characteristic of membranes of the smooth endoplasmic reticulum. These results are consistent with the contention that endoplasmic reticulum is a site of phenylpropanoid and flavonoid metabolism in Hippeastrum. The nature of bound forms of enzymes of phenylpropanoid and flavonoid metabolism have been investigated in Hippeastrum CV Dutch Red Hybrid. Particulate components of petal homogenates were fractionated on sucrose gradients and the EDTA shift method was employed to characterize membranes of the endoplasmic reticulum. In magnesium-containing gradients, a portion of phenylalanine ammonia lyase, chalcone synthase, glucosyl transferase, and all of the trans-cinnamate 4-mono-oxygenase and NADH Cytochrome c reductase (the last an endoplasmic reticulum marker) were associated with membranes equillibrating at 1.18 specific gravity. The results are consistent with the contention that endoplasmic reticulum is a site of phenylpropanoid and flavonoid metabolism in Hippeastrum . The nature of bound forms of enzymes of phenylpropanoid and flavonoid metabolism have been investigated in Hippeastrum CV Dutch Red Hybrid. Particulate compenents of petal homogenates were fractionated on sucrose gradients and the EDTA shift method was employed to characterize membranes of the endoplasmic reticulum. In magnesium-containing gradients, a portion of phenylalanine ammonia lyase, chalcone synthase, glucosyl transferase, and all of the trans-cinnamate 4-monooxygenase and NADH Cytochrome c reductase (the last an endoplasmic reticulum marker) were associated with membranes equilibrating at 1.18 specific gravity. In gradients lacking magnesium and containing EDTA, the above activities--except chalcone synthase, which was lost--and protein were diminished at 1.18 specific gravity and enhanced at lower densities characteristic of membranes of the smooth endoplasmic reticulum. These results are consistent with the contention that endoplasmic reticulum is a site of phenylpropanoid and flavonoid metabolism in Hippeastrum. |
| Author | Wagner G.J Hrazdina G |
| Author_xml | – sequence: 1 givenname: George J. surname: Wagner fullname: Wagner, George J. – sequence: 2 givenname: Geza surname: Hrazdina fullname: Hrazdina, Geza |
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| SubjectTerms | Biosynthesis Cytoplasm Cytosol endoplasmic reticulum Enzymes Flavonoids Hippeastrum Metabolism Particulate matter Petals Protoplasts Vacuoles |
| Title | Endoplasmic reticulum as a site of phenylpropanoid and flavonoid metabolism in Hippeastrum |
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