[Cow's milk protein intolerance: evaluation of immunological markers. A preliminary study]. / Intolleranza alle proteine del latte vaccino: valutazione di alcuni marcatori immunologici. Studio preliminare.

Cow's milk protein intolerance (CMPI) is recognised as an important cause of protean symptoms in infants. There are no tests with enough specificity and sensibility to set up a diagnostic assay. We carried out preliminary study on children suffering from CMPI with the following aims: a) to ascertain the importance of the variation in circulating antibodies to cow's milk proteins in CMPI, b) to establish a useful screening tool to diagnose CMPI. Seventy-four subjects (s.) were studied and divided into four diagnostic groups as follows: Six s. (3 M, 3 F) suffering from CMPI mean age 4.8 +/- 3.9 months, assuming a diet containing cow's milk: I group. Eleven s. (O M, 7 F) suffering from CMPI mean age 7.8 +/- 4.6 months, assuming a cow's milk free diet, for several months (mean 4.5 +/- 1.5): II group. Nine s. (5 M, 4 F) suffering from enteropathies not cow's milk correlated, mean age 18.5 +/- 10.6 months, assuming a diet containing cow's milk: III group. Fourty-eight healthy s. (24 M, 24 F), mean age 10.5 +/- 4.3 months, assuming a diet containing cow's milk.(ABSTRACT TRUNCATED AT 250 WORDS)

Serum IgA and IgG antibodies to alpha-gliadin: comparison between two ELISA methods.

We have developed two ELISA methods, i.e., enzyme immunoassay (EIA) and fluorescence immunoassay (FIA), for the semiquantitative detection of specific IgA and IgG antibodies directed against alpha-gliadin. The tests differ only for the enzyme substrate and, when optimized, could be used in large routine screening of celiac disease. Several serum samples from patients with celiac disease and gastrointestinal disorders as well as from control subjects were tested. Both methods gave good correlation with clinical data, were easily performed and had some specificity features, while FIA proved to be more sensitive.

Immunological characterization of the vitellogenic proteins in Squilla mantis hemolymph (Crustacea, Stomatopoda).

The femal specific proteins (FSP) identified in the hemolymph of Squilla mantis females are here proven to be vitellogenins (VTG) by immunological and electrophoretical methods. VTG 1 which has a higher molecular weight (MW) and only one central form, both in hemolymph and eggs, can be detected immunoelectrophoretically. VTG 2 and 3 have similar lower MW and are immunologically closely related, their slightly cathodic precipitation are fusing with the slightly anodic form. A further cathodic shift of the double arc occurs in the corresponding egg proteins. The VTGs are forms of yolk proteins which are transported in the hemolymph from the site of synthesis to the ovary where they undergo structural variations without involving a change of MW or of their number.

Wide-spectrum antibiotic activity of bovine granulocyte polypeptides.

The antibiotic activity of a polypeptide fraction purified from bovine granulocyte granules was tested against Escherichia coli, Pseudomonas aeruginosa, Salmonella typhimurium, Bacillus subtilis, Bacillus stearothermophilus, Staphylococcus aureus, Staphylococcus epidermidis, Streptococcus faecalis, Streptococcus pyogenes, and clinical isolates of Staphylococcus and Enterobacter spp. All of these bacterial species were susceptible to the antibiotic polypeptide(s), with MICs ranging from 3 to 100 micrograms of protein per ml. The antimicrobial activity was resistant to boiling and abolished by proteinase treatment. Saccharomyces cerevisiae and human fibroblasts grew normally in the presence of 100 and 50 micrograms of antibiotic polypeptide(s) per ml, respectively. [3H]thymidine incorporation into bacterial, but not fibroblast, DNA was efficiently and promptly inhibited by the antimicrobial polypeptide preparation. This suggests that its main target is a component of the system, which catalyzes and regulates the biosynthesis of bacterial DNA.

Morphological and molecular modifications induced by heat shock in Drosophila melanogaster embryos.

The early embryo of Drosophila melanogaster did not survive treatment at 37 degrees C (heat shock) for 25 min. The histological analysis of eggs treated in this way showed that the heat shock caused disintegration of nuclei and of cytoplasmic islands, displacement and swelling of nuclei and blocked mitoses. These effects were not observed in embryos treated after blastoderm formation. After this stage, we noticed that development was slowed down. The heat shock proteins (hsp 83, 70 and 68) were, under shock, synthesized at all developmental stages. There was little or no synthesis of hsp 70 and 68 in unfertilized eggs, but synthesis increased in proportion to the number of nuclei present. Most probably, hsp 70 synthesis was directed by zygotic mRNA. DNA synthesis was not blocked by the heat shock though the overall incorporation of [3H]thymidine was substantially reduced, presumably because of the block of mitoses. We did not find a direct relation between survival pattern and hsp synthesis. We concluded that some, at least, of the heat shock genes can be activated at all developmental stages and that heat shock could be used for synchronizing mitoses.