On the reconstruction of phylogenetic transformations. The origin of the arthropods

The conditions are outlined under which the body construction of annelids could have been transformed into that of arthropods. As an adaptation to a vagile life and an uptake of food by filtering particles from the sediment, the body was more and more flattened. Thus lateral protrusions, the subsequent pleurotergites, developed, and the parapodia were shifted to a more ventral position and could differentiate into the branched limbs typical for arthropods. This is the condition under which parts of the body wall were kept immobile, so that they could become sclerotized in the form of rigid plates.     

Studies in Heterobasidiomycetes,Part 38*)Sphacelotheca polygoni-persicariae G. Demi & Oberw. spec. nov.

A new species, Sphacelotheca polygoni-persicariae, parasitizing the ovaries of Polygonum persicaria L. is described. This smut, collected several times in Madeira, Portugal, differs from other species of that genus, by its host plant and the reticulated teliospore ornamentation. On the basis of the morphological and ultrastructural characters of S. polygoni-persicariae, in connection with some recently published data on siderophore formation and 5S ribosomal RNA sequences it can be assumed that 1) members of the genus Sphacelotheca are separated from typical Ustilago species of Poaceae, 2) Sphacelotheca is restricted to species parasitizing Polygonaceae, and 3) species of Sphacelotheca and Microhotryum as well as those Ustilago species which parasitize in the flowers of Polygonaceae are closely related.     

3',5'-Cyclic Adenosine Monophosphate- and Ca2+-Calmodulin-Dependent Endogenous Protein Phosphorylation Activity in Membranes of the Bovine Chromaffin Secretory Vesicles: Identification of Two Phosphorylated Components as Tyrosine Hydroxylase and Protein Kinase Regulatory Subunit Type II

Abstract: Membranes of the secretory vesicles from bovine adrenal medulla were investigated for the presence of the endogenous protein phosphorylation activity. Seven phosphoprotein bands in the molecular weight range of 250,000 to 30,000 were observed by means of the sodium dodecyl sulphate electrophoresis and autoradiography. On the basis of the criteria of molecular weight, selective stimulation of the phosphorylation by cyclic AMP (as compared with cyclic GMP) and immunoprecipitation by specific antibodies, band 5 (molecular weight 60,300) was found to represent the phosphorylated form of the secretory vesicle-bound tyrosine hydroxylase. The electrophoretic mobility, the stimulatory and inhibitory effects of cyclic AMP in presence of Mg²⁺ and Zn,²⁺ respectively, and immunoreactivity toward antibodies showed band 6 to contain two forms of the regulatory subunits of the type II cyclic AMP-dependent protein kinase, distinguishable by their molecular weights (56,000 and 52,000, respectively). Phosphorylation of band 7 (molecular weight 29,800) was stimulated about 2 to 3 times by Ca²⁺ and calmodulin in the concentration range of both agents believed to occur in the secretory tissues under physiological conditions.     

Viruspartikel im Siebröhrensaft von Cucumis sativus L. nach Infektion durch das Cucumisvirus 2 A

Summary Sieve tube sap obtained from cucumber plants infected by Cucumis Virus 2 A induced the typical mosaic disease when it was inoculated into healthy plants of the same species. The infectious factor could not be removed by dialysis or by treatment with phosphodiesterase. Therefore it is improbable that the virus is transported in the sieve tubes as low molecular units or as an unprotected RNA. Rod shaped particles (345×23 m) were found in the infectious sieve tube sap when it was investigated by electron microscopy. The same particles could be found in the sap extracted from infected leaves, but never in sieve tube sap obtained from healthy plants. There is reason to suppose that the Cucumis Virus 2 A is transported in the sieve tubes as complete particles.

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Einige Ergebnisse dieser Arbeit sind Teil einer Dissertation der Technischen Hochschule Darmstadt (D 17, 1964).