SIZE-ASSORTATIVE MATING IN A NATURAL POPULATION OF VIVIPARUS ATER (GASTROPODA: PROSOBRANCHIA) IN LAKE ZURICH, SWITZERLAND

The number of mating pairs, the size of the mating partners,and the distribution of individuals of Vivi-parus ater on agrid in Lake Zürich were recorded during one breeding seasonin 1990. There was positive assortative mating with respectto shell size. The proportion of copulating individuals rangedfrom 1% to 6% (average 3%) of the active population at any onetime. Individual snails copulated 60 times on average from Apriluntil November. Snails were abundant and copulated in shallowwater close to the shore in Spring. They moved towards deeperareas in Autumn. V. ater copulated on all substrates at anydepth (1–9 m)of the grid. The spatial distribution ofcopulations throughout the summer reflected the pattern of snailabundance. (Received 29 January 1993; accepted 14 November 1994)     

Physiological Adaptations in the Gastrointestinal Tract of Crayfish

SYNOPSIS. Crayfish are the dominant macrocrustacean in manyaquatic ecosystems and are the largest crustacean aquaculturalindustry in the United States, yet we know relatively littleabout their preferred and nutritionally important foods, aswell as their ability to utilize those foods. This review focuseson the ability of crayfish to detect foods, reduce food particlesize, digest macronutrients and the control of those functions.Of particular interest are the enzymatic capabilities of crayfish,especially trypsin, an alkaline protease, cellulase, muramidase,and possibly chitinase and chitobiase. The coordinated neuralcontrol of crayfish food location, ingestion and movement hasbeen well documented, while hormonal control mechanisms havenot. The conclusion we must draw from our current state of knowledgeis that crayfish have ample abilities to taste and locate potentialfoods and enzymatic adaptations developed in crayfish that allowuse of many of the foods they encounter in a benthic aquaticenvironment; other adaptations are lacking or have not beenelucidated.     

Membrane-protein interaction and the molten globule state: Interaction of α-lactalbumin with membranes

The insertion of soluble proteins into membranes has been a topic of considerable interest. We have studied the insertion of bovineα-lactalbumin into single-bilayer vesicles prepared from egg phosphatidylcholine (PC). Fluoresence studies indicated rapid and tight binding of apo-α-lactalbumin (apo-α-LA) to PC vesicles as a function of pH. The binding was maximal at pH values which favor the formation of the molten globule state. As an increase of hydrophobic surface is observed in the molten globule state, this conformational state can provide a molecular basis for insertion of soluble proteins into membranes. The membrane-bound complex formed at low pH (3.0) could be isolated and was found to be stable at neutral pH. The structural characterization of the apo-α-LA-PC complex was studied by fluorescence quenching using iodide, acrylamide, and 9,10-dibromostearic acid. The results obtained indicated that some of the tryptophans of apo-α-LA were buried in the membrane interior and some were exposed on the outer side. Fluorescence quenching and CD studies indicated the membrane-bound conformation of apo-α-LA was some conformational state that is between the soluble, fully folded conformation and the molten globule state.     

Some kinetic aspects and modelling of biotransformation of D-glucose to keto-D-gluconates

The bacterial oxidation of D-glucose to D-gluconic and keto-D-gluconic acids has been studied. Different approaches to pH-control have been checked. It is demonstrated, that the microbial growth is independent on pH-control. However, the rate of keto-gluconate production is too sensitive to the strategy of pH-maintenance and particularly to the neutralizing agent. The general opinion for the essential importance of addition of calcium ions for keto-gluconate formation is confirmed. The interpretation of the obtained experimental data by means of a simple mathematical model shows that the apparent lag-phase in keto-gluconate production is probably due to the necessity of accumulation of biomass as a biocatalyst and gluconic acids as a substrate.     

A recognition component of the ubiquitin system is required for peptide transport in Saccharomyces cerevisiae

Peptide transport in Saccharomyces cerevisiae is controlled by three genes: PTR1, PTR2, and PTR3. PTR1 was cloned and sequenced and found to be identical to UBR1, a gene previously described as encoding the recognition component of the N-end-rule pathway of the ubiquitin-dependent proteolytic system. Independently derived ubr1 mutants, like ptr1 mutants, were unable to transport small peptides into ceils. Concomitantly, ptr1 mutants, like ubr1 mutants, were unable to degrade an engineered substrate of the N-end-rule pathway. Further, ptr1 mutants did not express PTR2, a gene encoding the integral membrane component required for peptide transport in S. cerevisiae. These results establish a physiological role for a protein previously known to be required for the degradation of N-end-rule substrates. Our findings show that peptide transport and the ubiquitin pathway—two dynamic phenomena universal to eukaryotic cells—share a common component, namely UBR1/PTR1.