[Asymmetry of arterial blood pressure in the brachial artery in patients with cerebrovascular pathology].

Twenty-five patients suffering from cerebrovascular pathology coupled with arterial pressure (AP) asymmetry in the brachial arteries underwent an analysis including studies of the clinical picture, angiographic and rheographic readings (REG and RVG of the forearms and hands). It is demonstrated that revelation of a steady and well-defined asymmetry of AP in the brachial arteries associated with pulse weakening or disappearance in the radial artery on the side of AP decrease combined with pronounced asymmetry of the RVG readings for the forearms and hands is an important diagnostic and prognostic sign that points to the involvement into the process (occlusion or stenosis) of the subclavian artery. As a rule, this is coupled with lesions of the other main arteries of the head and may provoke impairment of the cerebral circulation, occurring more frequently in the arteries of the vertebrobasilar system.

[Quaternary structure of histidine decarboxylase according to small-angle x-ray diffraction and electron microscopic findings].

The data on small angle X-ray scattering with histidine decarboxilase (HDC) from Micrococcus sp. n. were analysed and a line of succesively improving approximations of the molecule shape was found: by oblate ellipsoid a:b:c = 1:10.

[Determination of the molecular weight and form of the molecule histidine decarboxylase by the method of small-angle x-ray scattering].

Shape and molecular weight of histidine-decarboxylase from Micrococus sp. n. were studied by the method of X-ray small-angle scattering.

[Specific modification of free lysine amino groups of histidine decarboxylase from Micrococcus sp. n. by trinitrobenzene sulfonic acid].

It has been found that 14 lysine residues are accessible for trinitrobenzene sulfonic acid (TNBS) in the molecule of histidine decarboxylase (HDC). The other 62 lysine residues in the molecule of native HDC are masked and inaccessible for TNBS. It is demonstrated that the SH- and alpha-amino groups of methionine are not modified by TNBS.

[Study of the structure of the histidine decarboxylase of Micrococcus sp. n. by the method of circular dichroism].

Ring dichroism spectra (RD) of histidine decarboxylase (HDC) from Micrococcus sp. n. at the regions of peptide bonds (200-240 nm) and aromatic amino acids (250-300 nm) absorption are studied.

[Flourescent properties of histidine decarboxylase from Micrococcus sp. n].

A dependency of fluorescence parameters of histidinedecarboxylase (HDC) from Micrococcuc sp. n. on pH values is studied.