A novel method for multiplex protein biomarker analysis of human serum using quantitative MALDI mass spectrometry.

In this work, we have extended our previously proposed approach for determining protein concentrations in human serum (using MALDI-TOF mass spectrometry) to include simultaneous analysis of several proteins associated with acute inflammation (alpha-2-macroglobulin, fetuin-A, serum amyloid A1). This technique can be used to diagnose systemic inflammation and provides results in 4-5 h. The developed approach was verified using standard immunological methods (ELISA).

[The morbidity with temporary disability and its regional characteristics in the Russian Federation in 2000-2018].

The article presents the results of analysis of dynamics of morbidity of working population with temporary disability in the Russian Federation in 2000-2018 according its causes, assessment of gender and age differences and in the context of Federal Okrugs and subjects The Russian Federation. The significant changes in rate and duration of temporary disability indices on National and Regional levels are considered. The absence of differences in structure of causes and average duration of morbidity with temporary disability is analyzed.

[The actual problems of planning of obstetric-gynecologic care in The Russian Federation].

The purpose of the study was to analyze normative legal documents and their modifications in order to determine the labor standards of medical personnel in case of rendering and planning obstetric gynecological care in the Russian Federation, including standards of number of medical personnel in medical organizations and modes of operation of various types. The materials of the study were normative legal documents presented at the WEB-portal "garant.ru".

A mass spectrometric approach to study the interaction of amyloid β peptides with human α-2-macroglobulin.

We used MALDI-MS to study the interaction of amyloid β (Aβ) peptides with alpha-2-macroglobulin (α2M). The binding of amyloid beta (Aβ) peptides to alpha-2-macroglobulin (α2M) was found to inhibit the ability of trypsin to cleave out the peptide α2M 705-715 (Pep-α2M) from α2M. This was observed with both purified α2M and α2M in human serum.

Quench me if you can: Alpha-2-macroglobulin trypsin complexes enable serum biomarker analysis by MALDI mass spectrometry.

One of the main functions of alpha-2-macroglobulin (A2M) in human blood serum is the binding of all classes of protease. It is known that trypsin, after such interaction, possesses modified proteolytic activity. Trypsin first hydrolyzes two bonds in A2M's 'bait region', and the peptide VGFYESDVMGR is released from A2M.