Protein-polysaccharide complexes as surfactants.

A study has been made of surface pressure (pi) and maximum shear stress (Ps) (at a constant shear rate) of decane-water interface on which bovine serum albumin (BSA) and its complexes with dextran sulfate (DS) were adsorbed. The pi values have been monitored by the Wilhelmy plate technique. The Ps values have been measured with a surface viscoelastometer. The changes of pi with time for BSA and BSA-DS complexes in general takes place in two stages which can be attributed to two corresponding limiting factors: diffusion of molecules (or particles) to the interface, and rearrangements of adsorbed molecules. The diffusion-controlled stage for the BSA-DS complexes was found to be several times as long as for BSA. The relaxation time of the second stage is a function of protein concentration Cp, for the complexes having maximum value at Cp = 10(-3)-10(-2) g/l. These maxima are coincident with midpoints of the surface pressure isotherms. The latter one of the BSA-DS complexes is shifted towards greater protein concentrations in comparison with that of BSA. The Ps assumes maximum values at Cp corresponding to the midpoints of surface pressure isotherms. These values for the complexes are 15-20 times greater the that for free BSA.

[Physico-chemical properties of the complexes of bacitracin with DNA and its effect on the process of transcription in vitro]. / Fiziko-khimicheskie svoistva kompleksov batsitratsina s DNK i vliianie ego na protsess transkriptsii in vitro.

The aim of the present paper was to study the action of one of the peptide antibiotics, bacitracin, as the regulator of gene activity at the transcription level. Therefore the commercial bacitracin has been fractionated into two main parts by paper chromotography. These two fractions have been identified as bacitracin A (biologically active) and bacitracin F (biologically inactive). The binding of both fractions to DNA has been studied. It has been shown that bacitracin A stabilizes DNA to a lesser degree than bacitracin F does. DNA-bacitracin complexes are formed in the major groove of the DNA helix by hydrogen bonds. The analysis of the the obtained experimental data allows us to suppose that bacitracin binding to DNA has a very specific character and that this antibiotic may act as the regulator of gene activity.