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1Author    Dietrich Werner, AndreasBernd WolffRequires cookie*
 Title    Root Hair Specific Proteins in Glycine max  
 Abstract    In root hairs from seedlings of Glycine max cultivars, isolated from the root system and com­ pared with the complete organ, specific soluble proteins have been found. By FPLC chromatogra­ phy and SDS gel electrophoresis root hair specific proteins with molecular weights of 13, 21, 34, 38 and 42 kDa were separated. Additionally, proteins with molecular weights of 12, 20, 69 and 74 kDa were significantly enriched in root hairs compared to roots without root hairs. By using CNBr activated Sepharose with antibodies against the root system without root hairs, the pres­ ence of root hair specific proteins was confirmed in extracts from isolated root hair cells. Enrich­ ment of Fe and Ca in some of the proteins from the root hairs is demonstrated. The present knowledge of the biochemical specificity of legume root hairs, the target cells of Rhizobium and Bradyrhizobium infection, is discussed. 
  Reference    Z. Naturforsch. 42c, 537 (1987); received October 7 1986 
  Published    1987 
  Keywords    Glycine max, Root Hairs, Roots, Specific Proteins, Infection 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0537.pdf 
 Identifier    ZNC-1987-42c-0537 
 Volume    42 
2Author    Petra Sperling, Ute Hammer, Wolfgang Friedt, Ernst HeinzRequires cookie*
 Title    High Oleic Sunflower: Studies on Composition and Desaturation of Acyl Groups in Different Lipids and Organs  
 Abstract    A selection o f lipids from achenes, cotyledons after germination, roots and leaves o f normal and high oleic varieties o f sunflower were analyzed with regard to their fatty acid profiles. The lipids included triacylglycerol and phosphatidylcholine as ER-made components and mono-and digalactosyl diacylglycerol as plastid-localized glycolipids. A comparison o f fatty acid pat­ terns showed that the block in oleate desaturation o f the high oleic variety is confined to the ER o f fat accumulating embryos, but that upon germination the oleate desaturation in the cotyledonary ER is rapidly derepressed. These data are supported by enzymatic experiments. In m icrosomes from maturing fruits o f the high oleic variety oleoyl-phosphatidylcholine de-saturase could not be detected, whereas o leo y l-C o A : lyso-phosphatidylcholine acyltransferase and com ponents o f the microsomal electron transport chains were not affected. A correlation in the expression o f desaturation blocks in seed and root fatty acids as observed in mutants o f other species was not observed which, therefore, cannot be generalized. Our data are discussed in terms o f the existence o f two ER-specific oleate desaturase activities. 
  Reference    Z. Naturforsch. 45c, 166 (1990); received November 20 1989 
  Published    1990 
  Keywords    Triacylglycerols, G alactolipids, Phosphatidylcholine, Cotyledons, Leaves, Roots 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-0166.pdf 
 Identifier    ZNC-1990-45c-0166 
 Volume    45 
3Author    CarolinaG. Casado, A.Ntonio HerediaRequires cookie*
 Title    Water Permeability of Hypodermis Isolated from Clivia miniata Roots  
 Abstract    The fine structure and water permeability of hypoder­ mis isolated from roots of Clivia miniata have been studied. The hypodermis is composed of five layers of cells arranged in radial rows. The cell walls of these lay­ ers consist of primary and tertiary walls and suberized secondary walls which are lamellated. Water perm eabil­ ity of the isolates was low, around the value of 10^9 m s-1. This value was found independent of the pH solu­ tion and of the ionic exchange capacity of the isolates. Suberin extraction increased water permeability one or­ der of magnitude. 
  Reference    Z. Naturforsch. 53c, 1096—1099 (1998); received July 29/September 7 1998 
  Published    1998 
  Keywords    Root, Hypodermis, Suberin, Water Permeability, Ionic Exchange Capacity 
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 TEI-XML for    default:Reihe_C/53/ZNC-1998-53c-1096_n.pdf 
 Identifier    ZNC-1998-53c-1096_n 
 Volume    53 
4Author    Ralf Perrey, Marie-Theres Hauser, MichaelW. InkRequires cookie*
 Title    Cellular and Subcellular Localization of Peroxidase Isoenzymes in Plants and Cell Suspension Cultures from Lupinus polyphyllus  
 Abstract    , leaf protoplasts and cell suspension cultures of Lupinus polyphyllus and isolated vacuoles were studied for cellular and subcellular localization of peroxidase isoenzymes. Isoelectric focusing revealed 16 peroxidase isoenzymes. The basic peroxidase isoenzymes are predominantly localized in the vacuole and, to a minor degree, unbound in the intercellular space. The acidic isoenzymes are cell wall-bound in plants and not detectable in suspension-cultured cells. Large amounts (up to 11.0 U/ml) of a single basic isoenzyme are detectable in the spent medium of cell suspension cultures. 
  Reference    Z. Naturforsch. 44c, 931—936 (1989); received August 4 1989 
  Published    1989 
  Keywords    Lupinus, Peroxidase, Localization, Isoelectric Focusing (Peroxidase), Cell Culture Leaves, stems, roots 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0931.pdf 
 Identifier    ZNC-1989-44c-0931 
 Volume    44