Seasonal variations in gross biochemical composition, percent edibility, and condition index of the clam Ruditapes Decussatus cultivated in the Ria Formosa (South Portugal)

The grooved carpet shell clam, Ruditapes decussatus (L. 1758), is one of the most popular and profitable molluscs exploited in rearing plots in the Mediterranean. However, annual catch has been declining steadily since the early nineties. In order to understand the seasonality of its nutritional value, thus providing an improved basis for economical valuation of the resource, gross biochemical composition, percentage edibility and condition index were investigated during a year with monthly periodicity in a commercially exploited population of the clam Ruditapes decussatus in the Ria Formosa, a temperate mesotidal coastal lagoon located in the south of Portugal. Our results show that total and non-protein nitrogen co-varied during the year, resulting in a protein content that peaked in the warmest months. Although complementary in summer, carbohydrate and lipid contents showed irregular annual trends. The observed seasonality was comparable to that shown by studies elsewhere at similar latitudes, and are underpinned by the reproductive cycle of the species. Our results show the clams to be at their prime nutritional value at the beginning of summer, when protein content peaks.

The effect of sucrose on protein stability and fibrillation of prion and S6 protein

Aggregation and fibrillation of proteins have a great importance in medicine and industry. Misfolding and aggregation are the basis of many neurodegenerative diseases like Alzheimer and Parkinson. Osmolytes are molecules that can accumulate within cells and act as protective agents and they can inclusively act as protein stabilizers when cells are exposed to stress conditions. Osmolytes can also act as protein stabilizers in vitro. In this work, two different proteins were studied, the ribosomal protein from Thermus thermophilus and the mouse prion protein. The existence of an unstructured N-terminal on the prion protein does not affect its stability. The effect of the osmolyte sucrose on the fibrillation and stabilization of these two proteins was studied through kinectic and equilibrium measurements. It was shown that sucrose is able to compact the native structure of S6 protein in fibrillization conditions. Sucrose affects also folding and unfolding kinetic of S6 protein, delaying unfolding and increasing folding rate constants. The mechanism of stabilization by sucrose is non-specific because it is distributed for all protein structure, as it was demonstrated by a protein engineering approach. Sucrose delays the process of formation and elongation of S6 and prion protein from mouse. This delay is the result of the compaction of the native structure refered above. However, cellular toxicity studies have shown that fibrils formed in the presence of sucrose are more toxic to neuronal cells.

Molecular cloning, full-length sequence and preliminary characterization of a 56-kDa protein induced by human interferons

Among the various proteins which are induced when human cells are are treatened with interferon, a predominant protein of unknown function, with molecular mass 56 kDa, has been observed. With the aim of exploring the molecular basis of the regulation of this protein and of its mRNA, in order to understand its biological functionand its possible contribution to the various antiviral and non-antiviral actions exerted by interferons.