Pachypteria sinaitica n. sp. - eine aufgewachsene,austernähnliche muschel aus dem unterkarbon Ägyptens

A pseudomonotide pelecypod-Pachypteria sinaitica n. sp. - is described from Abu Durba Formation (Visé) of southwest Sinai. The new species forms a link with rather similar populations in the Lower Carboniferous of Marocco. Like the oysters, but byssate and cemented with its right valve,P. sinaitica n. sp. built up small limestone beds within a marginal marine environment of sedimentation. As regards the isotopie composition, the carbonates of the shell were secreted in a water of approximately 25° C.It follows, that the littoral waters of the southern Tethys were warmer during the Lower Carboniferous than those of present Red Sea.     

Imino proton assignments in the proton nuclear magnetic resonance spectrum of the lambda phage OR3 deoxyribonucleic acid fragment

The 17 base pair duplex d(TATCACCGCAAGGGATAp) . d(TATCCCTTGCGGTGATAp) corresponding to the OR3 operator site of lambda phage has been synthesized and studied by 1H nuclear magnetic resonance spectroscopy at 470 MHz. The 13 imino proton resonances observed at 20 degrees C have been assigned to specific base pairs at positions 3-15 on the basis of nuclear Overhauser effect measurements and studies of the temperature dependence of peak intensities. Resonances from the A-T base pairs at positions 1, 2, 16, and 17 are assumed to be absent from the spectrum because of terminal fraying. Resonance from many of the base pairs suggested by Ohlendorf et al. [Ohlendorf, D. H., Anderson, W. F., Fisher, R. G., Takeda, Y., & Matthews, B. W. (1982) Nature (London) 298, 718-723] to be involved in specific binding of the lambda phage cro repressor are well resolved.     

Chromosomen-Aktivität und biochemische Zelldifferenzierung in den Speicheldrüsen von Camptochironomus

Salivary glands of Camptochironomus tentans and C. pallidivittatus were used to study the question whether genes controlling the synthesis of characteristic cell proteins are located in chromomeres specifically puffed in this tissue. Salivary gland cells produce considerable amounts of secretory proteins. In G. tentans, this secretion was shown by gel electrophoresis to consist essentially of 5 protein subunits. In C. pallidivittatus, a component (no. 6) additional to these was found. Another constituent of the secretion (no. 7) is synthesized in C. pallidivittatus by only a small group of gland cells. — The inheritance of these species- and cellspecific proteins has been investigated by relating their presence in interspecific hybrids to the chromosome constitution. Fraction no. 6 was found to be correlated to a short distal region of chromosome IV in which a tissue-specific Balbiani ring is located. Secretion component no. 7 which is characteristic of the special gland lobe of C. pallidivittatus is also controlled by chromosome IV which in this lobe develops a cell-specific Balbiani ring.

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Herrn Professor Dr. W. Beermann bin ich für die Anregung zu dieser Arbeit, sein stetes, förderndes Interesse und die Überlassung aller Arbeitsmöglichkeiten zu großem Dank verpflichtet. Ferner möchte ich Herrn E. Freiberg für das verständnisvolle Ausführen der Zeichnungen und Herrn Peinmechanikermeister H. Braun für seine vielfältige Hilfe herzlich danken.     

Callus cultures of tomato mutants: I. Nutritional requirements

Callus from hypocotyl, stem, and fruit tissue of tomato mutants was grown on a complex pea extract medium. The genotypes responded differently to the levels of nutrients and stimulators or inhibitors in the medium. Hypocotyl callus of yellow (r) tomato required K(2) SO(4) for quick establishment and continued steady growth for several months; callus of this mutant could also grow with 0.5 % dimethyl sulfoxide in the medium, although growth was less than the control. The red ghost (r(+) gh) mutant is sensitive to a toxic component in the pea extract, and makes its best growth with the standard minerals and vitamins, but in 1/2 concentration pea extract plus 5 % coconut water. Tangerine (t), red lutescent stem (r(+) l(2) ), and r(+) gh are mutants which respond differently to thiourea: t grows about the same at all concentrations, r(+) gh grows best at low thiourea, and r(+) l(2) grows best at the specific level of 20 mg/l thiourea. The recent active t or r(+) l(1) and r(+) l(2) isolates require supplementary auxin to which the older, slow-growing isolates do not respond. However, there is variation in growth response of different isolates of the same mutant. The several red (r(+) ) cultures are similar in their slow growth, but somewhat different in responses to specific nutrients. The recent (+) isolate is one of the most active cultures, in comparison to the slow growth of t callus isolated in 1964. It is therefore concluded that growth is affected both by the specific requirements of the mutant and by the age and vigor of isolates.     

Über Aufbau und Innervation der Kopfanhänge der prosobranchen Schnecken

Zusammenfassung Das Epithel der Kopfanhänge von elf marinen und Süßwasserprosobranchiern besteht aus prismatischen bis kubischen Stützzellen mit meist dichtem Mikrovillussaum und z.T. Pigmentgranula sowie Sinneszellen, die fast immer in Form sekundärer Sinneszellen vorliegen; nur bei Patella coerulea kommen vermutlich auch primäre Sinneszellen vor. Ihr Zytoplasma ist apikal durch glattwandige E. R.-Zisternen, helle Bläschen und Mikrotubuli gekennzeichnet. Außerdem tragen diese Zellen Zilien und stehen basal mit Nervenendigungen in Kontakt, die sich in drei Gruppen einteilen lassen: 1. Vermutlich cholinerge Endigungen mit optisch leeren Bläschen (Ø 600–800 Å). 2. Endigungen mit dense core vesicles (Ø 1000–1100 Å). Die Annahme, daß diese Endigungen biogene Amine enthalten, wird durch fluoreszenzmikroskopische Befunde gestützt. 3. Endigungen mit großen (Ø 3000–4000 Å) neurosekretorischen Elementargranula.

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Structure and innervation of the cephalic tentacles of Prosobranch molluscs

Summary The epithelium of the cephalic tentacles of eleven marine and freshwater prosobranch snails consists of villus bearing supporting cells, which partly contain pigment granules, and sensory cells, which occur in form of secondary sensory cells with the exception of Patella coerulea which presumably possesses primary sensory cells. These receptor cells are characterized as chemoreceptors by apical cilia, smooth surfaced E.R., microtubulues and empty vesicles. At their bases they are in close contact with nerve endings which can be classified in three groups: 1. presumably cholinergic endings with clear vesicles (Ø 600–800 Å). 2. endings with dense core vesicles (Ø 1000–1100 Å). The assumption that these endings contain biogenic amines is supported by positive fluorescence microscopical tests. 3. Endings with big (Ø 3000–4000 Å) neurosecretory elementary granules.

Herrn Prof. Dr. W. Bargmann danke ich für die Überlassung eines Arbeitsplatzes im Anatomischen Institut Kiel.     

Der Turnover der Proteine in den Organen des Flußkrebses Orconectes limosus

Zusammenfassung Aus dem exponentiellen Abfall der spezifischen Aktivität nach einmaliger Injektion von L-Leucin-¹⁴C wurden die Halbwertszeiten der Gesamtproteine in den meisten Organen des Mußkrebses zu 8,5–19 Tagen bestimmt, in Leber und Niere der Maus zu 1,6–1,7 Tagen. Muskel- und Hämolymphproteine des Krebses zeigten weit längere Halbwertszeiten. Berücksichtigt man die Temperaturdifferenz von 25° unter Annahme eines Q ₁₀ von 2,0–2,5, so ergeben sich für Maus und Krebs etwa übereinstimmende Geschwindigkeiten des Proteinturnovers.

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Protein turnover in the tissues of the crayfish, Orconectes limosus

Summary The exponential decay of protein radioactivity after injection of L-Leucin-¹⁴C was measured in the different tissues of the crayfish, and in liver and kidney of the mouse. The half life time of tissue proteins was calculated to be 8.5 to 19 days in most crayfish tissues, 1.6 to 1.7 days in the mouse liver and kidney. Proteins of muscle and hemolymph of crayfish had much longer half life values. Taking into consideration the temperature difference of 25° C and assuming a Q ₁₀ of 2.0 to 2.5, the speed of protein turnover corresponds in the mouse and the crayfish.

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Mit Unterstützung der Deutschen Forschungsgemeinschaft.