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'Oocytes' in keywords
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1985 (1)
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1976 (1)
1Author    Rüdiger RiehlRequires cookie*
 Title    Pomatoschistus minutus III. Determination of Amino Acid Component  
 Abstract    The oocytes of the marine goby Pomatoschistus minutus were analyzed for their amino acid content. Most of the amino acids exist as protein, only a little part is free or peptide-bound. Among the protein-bound amino acids, high levels of glutamic acid, proline, alanine, aspartic acid, valine and leucine were detected. These represent more than 60% of the protein amino acids. Among the free acids, glutamic acid, serine and alanine, are dominant. There are no certain proofs o f the occurrence o f peptide pools in the oocytes o f Pomatoschistus minutus. 
  Reference    Z. Naturforsch. 35c, 1094—1095 (1980); received June 9/July 16 1980 
  Published    1980 
  Keywords    Oocytes, Yolk, Amino Acid Component, Pomatoschistus minutus, Teleost 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-1094_n.pdf 
 Identifier    ZNC-1980-35c-1094_n 
 Volume    35 
2Author    Rüdiger Riehl, Volker WalldorfRequires cookie*
 Title    Raillietiella aegypti (Pentastomida, Cephalobaenida)  
 Abstract    The oocytes of the cephalobaenid Pentastomid Rail­ lietiella aegypti were studied by electron microscopy. A prominent feature of vitellogenic oocytes are numerous spherical, oval and elongated mitochondria. Some of these are shown with desmosome-like structures. The associa­ tions between mitochondria and the desmosome-like struc­ tures have always been observed to lie freely in the oocyto-plasm; there are no apparent connections with the oocytous plasma membrane. Possible functional roles of these com­ plexes are evaluated. 
  Reference    Z. Naturforsch. 40c, 748—750 (1985); received July 10 1985 
  Published    1985 
  Keywords    Oocytes, Mitochondria, Desmosome-like Structure, Rail­ lietiella aegypti, Pentastomida 
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 TEI-XML for    default:Reihe_C/40/ZNC-1985-40c-0748_n.pdf 
 Identifier    ZNC-1985-40c-0748_n 
 Volume    40 
3Author    Riidiger RiehlRequires cookie*
 Title    Eine A Special Attaching-Mechanism between the Cortex radiatus externus and the Follicle Epithelium of the Oocytes of Gobio gobio  
 Abstract    besondere Haftvorrichtung zwischen Cortex radiatus externus und Follikel­ epithel der Oocyten von G obio g o b io (L). The cortex radiatus externus and the follicle epithelium of the freshwater teleost Gobio gobio are firmly attached together by a special attaching-mechanism. The apical surface of the plugs of the cortex radiatus externus has recesses and excavations which fit in the short projections of the follicle cells and prevent moving of these cells on the egg mem­ branes. This attaching-mechanism also assists in fastening the oocytes (eggs) on the substrate. 
  Reference    (Z. Naturforsch. 31c, 628 [1976]; eingegangen am 23. Juni 1976) 
  Published    1976 
  Keywords    Electron Microscopy, Gobio gobio, Oocytes, Cortex radiatus externus, Attaching-Mechanism 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0628_n.pdf 
 Identifier    ZNC-1976-31c-0628_n 
 Volume    31 
4Author    Riidiger RiehlRequires cookie*
 Title    Parakristalline Körper in jungen Oocyten der Schmerle  
 Abstract    N o em a ch eilu s barbatulus (L.) (Teleostei, Cobitidae) Paracristalline Bodies in Young Oocytes of the Loach, Noemacheilus barbatulus (L.) (Teleostei, Cobitidae) Young oocytes of the loach, Noemacheilus barbatulus (L.), were studied by electron microscopy. Fistular paracristalline bodies are found in the oocytes during state I. They consist of many osmiophilic particles with a diameter of 150 — 300 A. Ultrahistochemical experiments have demonstrated that the paracristalline bodies are mainly composed of pro­ teins. The paracristalline bodies are yolk precursors. 
  Reference    (Z. Naturforsch. 32c, 305 [1977]; eingegangen am 26. Januar 1977) 
  Published    1977 
  Keywords    Paracristalline Bodies, Oocytes, Yolk Precursors, Electron Microscopy, Noemacheilus barbatulus 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0305_n.pdf 
 Identifier    ZNC-1977-32c-0305_n 
 Volume    32