Serum albumin fragmentation in end-stage renal disease patients--a pilot study.

Background: The goal of this study was to detect modification in the expression of plasma proteins and/or post-translational modifications of their structure in patients with end stage renal disease.

Methods: Serum samples from 19 adult patients treated by maintenance hemodialysis (MHD) were analyzed in comparison to sera from six healthy controls using sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimensional electrophoresis (2DE). Spots of interest were identified by mass spectrometry analysis.

Effects of the incubation in vitro with sorbents on serum proteomic pattern and cytokine concentration in cancer patients during chemotherapy--preliminary results.

Introduction: Cancer and treatment by chemotherapy often produce abnormalities in endogenous cytokine, chemokine, and inflammatory mediator production. Sorbent-based adsorption therapies have been used to remove cytokines in diverse human diseases.

Aim: The aim of this study was to evaluate the effects of chemotherapy on serum proteomic pattern and cytokine concentration, and to evaluate the ex vivo feasibility of using sorbents to remove cytokines, chemokines and other proteins in adult cancer patients undergoing chemotherapy with fluorouracil or carboplatin-taxane combinations.

Towards royal jelly proteome.

The recent availability of the honey-bee Apis mellifera genome and trascriptome of both the female castes, has stimulated new efforts in investigating the protein composition of royal jelly (RJ), its role in caste differentiation and its quality and typicality by a proteomic approach. This study is aimed both to separate and identify proteins of royal jelly and to detect some of them in honey-bee pollen-bread by using two-dimensional gel electrophoresis, mass spectrometry and by de novo sequencing. All the identified proteins belonged to the Apis mellifera genome.

Characterisation of a specific phycocyanin-hydrolysing protease purified from Spirulina platensis.

A novel protease has been identified, purified and partially characterised from complete medium grown Spirulina platensis, which could be responsible for the selective proteolysis of phycobiliproteins. It is an 80 kDa homodimeric enzyme; its N-terminal sequence is not related to any known protease sequence. It hydrolyses native phycocyanins in both crude extracts and reconstructed systems with purified Allo- or C-phycocyanin.