Digestion of chlorophylls and carotenoids by the marine protozoan Oxyrrhis marina studied by h.p.l.c. analysis of algal pigments

Algal pigments were measured, by reverse-phase h.p.l.c., duringgrazing experiments with the protozoan Oxyrrhis marina Dujardinon Rhodomonas sp. Chlorophylls and carotenoids were degradedto colourless residues; the rate of degradation of pigmentswas highest in the light. Very little chlorophyll a (5%) wasdegraded to phaeophytin and none to phaeophorbide during grazing.This suggests that phaeopigment concentrations cannot be usedas a measure of algal mortality due to grazing when heterotrophicProtozoa are a component of the grazer community.     

The role of the Escherichia coli λ receptor in the transport of maltose and maltodextrins

The λ receptor is a peptidoglycan-associated integral protein that spans the outer membrane. Beside its function in phage λ adsorption it participates in transport. The latter function can be summarized as follows: (1) Receptor allows the nonspecific permeation of small molecules other than maltose and maltodextrins (in close analogy to a molecular sieve). Here the only criterion for selectivity is size and it has the properties of an unspecific pore. In this respect, it is similar to the outer membrane proteins Ia, Ib, and Ic, the porins. (2) It is a binding protein for maltodextrins. Binding affinity is low but increases by a factor of 500 as the chain length of the maltodextrins increases. In contrast, the affinity of the periplasmic maltose-binding protein for maltose and maltodextrins is similarly high (in the μM range). (3) In the in vitro system of liposomes, the λ receptor facilitates specifically the diffusion of maltodextrins that exceed the size limit given by its porin function. This clearly demonstrates that the λ receptor alone is able to specifically overcome the permeability barrier of the outer membrane for maltodextrins. (4) From the genetic and kinetic analysis of maltose and maltodextrin transport, it can be concluded that the λ receptor interacts with the periplasmic maltose-binding protein. (5) Electron microscopic studies indicate a location for the maltose-binding protein in the outer cell envelope. This location is dependent on the presence of the λ receptor.     

Glutamate dehydrogenase from Pisum sativum L.

A 2–8-fold increase in the activity of glutamate dehydrogenase (GDH), accompanied by an alteration of the GDH isoenzyme pattern, was observed in detached pea shoots floated on tap water (preincubated shoots). Sugars supressed the process, whereas NH ₊ ⁴ and various metabolites as well as inhibitors of energy metabolism and protein synthesis were ineffective. The subcellular distribution pattern revealed evidence that the GDH isoenzymes are exclusively located in the mitochondrial matrix. The alterations in GDH activity occurring in preincubated shoots are restricted to the mitochondria.An experimental device suitable for studying the GDH function in isolated intact mitochondria has been established. Using [¹⁴C] citrate as the carbon source and hydrogen donor, the mitochondria synthesized considerable amounts of glutamate upon addition of NH ₊ ⁴ . The rates of glutamate formation in dependency of increasing NH ₊ ⁴ levels follow simple Michaelis-Menten kinetics. Half-saturation concentrations of NH ₊ ⁴ of 3.6±1.2 mM; 1.9±0.06 mM and 1.6±0.1 mM were calculated for the mitochondria isolated from pea shoots, roots, and preincubated shoots, respectively. The results are discussed in relation to the possible role of GDH in NH_+/4 assimilation at elevated intracellular NH_+/4 levels.Abbreviations GDH Glutamate dehydrogenase - MDH malate dehydrogenase - GOT aspartate aminotransferase - SDH succinate dehydrogenase - HEPES 4-(2-hydroxyethyl)-1-piperazineethan-sulfonic acid - BSA bovine serum albumin - TPP thiamine pyrophosphate - DNP 2,4-dinitrophenol - CCCP carbonyl cyanide m-chlorophenylhydrazone - DCPIP 2,6-dichlorophenolindophenol Dedicated to Professor Dr. Maximilian Steiner on the occasion of his 75th birthday     

Palaeoecology of coralline sponge-coral meadows from the upper jurassic of Portugal

TheComophyllia polymorpha-Crispispongia cf.expansa association of the Kimmeridgian Alcobaça Formation occurs in a 5–10 m thick unit that can be followed for at least 10 km in the vicinity of Alcobaça (Estremadura). Corals, coralline sponges (mainly Calcarea), cryptalgal crusts and, to a lesser extent, crinoids are the dominant constituents of the autochthonous community relic which can be grouped in framebuilders, framework encrusters, frame binders, reef-dwellers, and reef destroyers. These organisms formed low meadows in a shallow, fully marine environment subject to low rates of sedimentation and moderate to low energy levels punctuated by rare high energy events. The abundance of coralline sponges in reefs and reef-like communities is uncommon in the Jurassic and appears to be restricted to very shallow water environments.