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S Marinoni

Publications and source records attributed to S Marinoni.

22 records · Page 2Linked to original sources

[Changes in the immunologic profile of newly-diagnosed diabetic patients during the first year of the disease].

Immunological markers including ICA-IgG, CF-ICA, other non organ specific autoantibodies, circulating immune complexes (CIC), IgG, IgA, IgM, C3, C4 and lymphocyte subpopulations (OKT3, OKT4, OKT8) were studied at onset in 32 insulin dependent diabetic patients (16 males, 16 females, aged 1-21 yr.). Other non organ specific autoantibodies, CIC, IgG, IgA, IgM, C3, C4 and OKT3, OKT4, OKT8 were also studied after a 6-12 months follow-up in the same group of patients. ICA-IgG and CF-ICA were also studied in a control group of 19 insulin dependent diabetic patients with an over 3 year history of diabetes. ICA IgC, CF-ICA, other autoantibodies and CIC were detected at diagnosis in 65%, 19%, 33%, and 50% of patients respectively. ICA-IgG and FC-ICA were detected respectively in 15% and zero of the control group of 19 long standing diabetes. No alterations in IgG, C3 and C4 levels and in T cells subsets have been found at onset. C4 levels significantly decreased at the successive observation. A significant elevation of IgG levels and helper/suppressor ratio were also observed at follow-up. Autoantibodies and CIC positive sera at diagnosis support the concept that a previous autoimmune disorder exists before clinical manifestations of diabetes. Other immunological abnormalities including relative hypogammaglobulinemie, lower C4 and higher helper/suppressor ratio, observed by other authors (Kanakoudi 1984, Vergani 1985, Lernmark 1985) represent an aspecific alteration due to metabolic imbalance or to an earlier immunological disorder.

Adolescent↗

Purification of glucose-6-phosphate dehydrogenase from rabbit reticulocytes by immunoaffinity chromatography.

Glucose-6-phosphate dehydrogenase (G6PD) was purified from rabbit reticulocytes by using a single immunoaffinity chromatographic step. Antibodies against rabbit erythrocyte G6PD were raised in a goat, purified near to homogeneity and immobilized on CarboLink gel (Pierce). Nonspecific binding sites on the matrix were saturated with myokinase from rabbit muscle. Reticulocyte lysate was directly loaded onto the column, allowed to enter the gel bed and incubated for 15 min at room temperature. The column was washed first with PBS and then with 1 M NaCl. The enzyme was eluted with 0.1M acetic acid in 1M NaCl. Two protein bands of about 66.2 kDa were co-eluted with the G6PD, which was however well separated in SDS-PAGE. The eluent destroyed the enzyme activity but the G6PD yield was higher than 90%.

Animals↗