[Effect of 1 month's treatment with Bezalip on the serum lipids and lipoproteins of patients with different types of hyperlipoproteinemias]. / Vliianie na ednomesechno lechenie s Bezalip vurkhu serumnite lipidi i lipoproteini pri bolni s razlichni tipove khiperlipoproteinemii.

The effect of one-month bezalip (600 mg daily) outpatient department treatment was studied on serum lipids and lipoproteins of 34 patients (31 males and 3 females), aged from 30 to 60 with various types primary HLP (IIA, IIB, IV and V). After the treatment, it was established that tendency to malization of the increased concentrations of triglycerides (Tg) and cholesterol (Chol) was changed. The drug has a stronger effect on triglyceride component of serum VIDLP and LDLP as compared with the corresponding cholesterol one, due to which its treatment is with better effect in IIB, IV and V type HLP. The decrease of cholesterol concentration in the separate types HLP differs in size and mode of induction. It is stronger in the mixed types HLP (II phi and V) and is due to decreased cholesterol content of LDLP and VLDLP, whereas in IIb type HLP - the serum concentrations of total Chol was decreased as well as of LDLP-Chol with a parallel increase of the levels of LVDLP-Chol and VLDLP-Tg. In IIA and V type HLP, serum concentration of HDLP-Chol is increased but insignificantly. Bezalip treatment changes the interlipoprotein index Ka (total Chol-HDLP-Chol/HDLP-Chol) in a favourable direction as regards the atherogenic risk, in all types HLP studied.

[Insulin receptors in isolated cells of murine lactating mammary gland]. / Insulinovye retseptory v izolirovannykh kletkakh laktiruiushchei molochnoi zhelezy myshei.

Insulin receptors in isolated cells from lactating mouse mammary gland were investigated by 125I-labeled insulin. A modified chloramin T-method after Hunter and Greenwood (1962) was used for insulin labelling with 125I; 125I-insulin with a high specific activity (80--120 muCi per microgram), high immunoreactivity and preserved biological properties was obtained. Three methods of labeled insulin purification were also studied: absorption on the cellulose column, gel chromatography on different types of Sephadex (G-25, G-75, G-100) and electrophoresis on polyacrylamide gel. The best conditons for iodination and purification of 125I-insulin suitable for studying the receptor-insulin binding in the isolated cells from mouse mammary gland were selected. Insulin binding to its receptor was found to be a specific reversible process, having high affinity and a tendency to saturation. The receptor-insulin-binding equilibrium was reached in 30 min at 24 degrees C. Specific binding was observed at a very low concentration of 125I-insulin (0.4.10(-9)M), close to the physiological level. Saturation was observed at a concentration of over 1.5.10(-9)M. Native, non-labeled insulin, at a concentration of 1 ng per ml lowered the labeled insulin binding by 10--20 per cent, whereas 10 ng per ml led to a 60 per cent lowering. The affinity constant of the process was about 10(9).M-1. Each cell had about 3 000 to 4 000 insulin binding sites.