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Biomedical subjects

S M Klimenko

Publications and source records attributed to S M Klimenko.

At least 73 records · Page 4Linked to original sources
PubMedDate not supplied

[Structure and regulation of the assembly of bacteriophage T4 fibrillar proteins. II. Isolation and initial structural characteristics of whiskers].

A procedure for purification of bacteriophage T4 whiskers and it's monomeric subunits--gene product wac--has been developed. We have shown, that the whiskers are composed of two identical copies of gene product wac with molecular weight of 56 kDa each. The dimer of gene product wac is a highly ordered structure and it's length is about 70.0 +/- 10.0 nm, as revealed by electron microscopy. The amino acid composition of whiskers is very similar to that of watersoluble keratins. We have proposed a new term for the definition of the whiskers--the fibritin.

Chromatography, Gel↗
PubMedDate not supplied

[Electron microscopic study of Lassa virus].

Ultrafiltration through hollow fibrous filters followed by purification in interrupted and linear urografin gradients yielded a Lassa virus suspension of high concentration. The use of gamma-irradiation for inactivation of the frozen virus suspension (-70 degrees C) caused no apparent structural changes of virions and made it possible to examine Lassa virus in electron microscope by negative staining. The observed virus particles in their morphology and sizes did not differ from previously described particles of other members of the Arenaviridae family. In ultrathin sections of Lassa virus-infected Vero cells, atypical virions were sometimes visible alongside with typical particles. Within one type of such particles no ribosome-like granules could be detected. Such "hollow" particles may possibly be defective virions. Another kind of atypical particles contained homogeneous electron-dense core and resembled mycoplasma. Of greatest interest are the particles with heterogeneous core in which "sandy" granules can be distinguished. The presence of greater amounts of uranophilic material than usually may be explained by getting into the virion in the process of its formation of a greater amount of genetic material than that present in typical virions.

Animals↗
PubMedDate not supplied

[Possibility of detecting the matrix protein of the influenza virus in intact and disrupted virions by immunoenzyme analysis and immune electron microscopy].

ELISA and immune electron microscopy were used to study possible causes of the detection of antigenic reactivity of influenza virus matrix protein in purified virus suspension directly adsorbed on polystyrene. No interaction of antibody to M protein with the surface of virus and subvirus particles was observed. The process of virus sorption on polystyrene for a long period was shown not to lead to disruption of intact virus particles, and the detection of the internal matrix protein in preparations of purified influenza virus was due only to the presence of partially or completely destroyed virions in the viral suspension.

Absorption↗