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1.
Vopr Virusol ; 56(2): 4-9, 2011.
Artigo em Russo | MEDLINE | ID: mdl-21545032

RESUMO

Research Institute of Influenza, Ministry of Health and Social Development of Russia, Saint Petersburg The characteristics of the isolation of pandemic influenza A(H1N1)v viruses were studied on chick embryos (CE) and MDCK cell culture. The materials (nasal swabs and autopsies) were collected in different regions Russia in the period from 20 July to 30 December 2009. The paper gives the data of the antigenic analysis of isolates, their capacity to multiply in different species-specific and tissue cell cultures. The viruses isolated on CE were shown to have higher hemagglutination titers and to be more stable. Isolation from the autopsies was effective only on CE. All the test cell lines other than MDCK were insensitive to the isolated pandemic influenza strains. The antigenic analysis showed no significant antigenic drift of the viruses isolated during the first wave of the pandemic in the Russian Federation.


Assuntos
Antígenos Virais/análise , Vírus da Influenza A Subtipo H1N1 , Influenza Humana , Animais , Anticorpos Antivirais , Variação Antigênica , Antígenos Virais/imunologia , Antígenos Virais/isolamento & purificação , Técnicas de Cultura de Células , Linhagem Celular , Embrião de Galinha , Cães , Testes de Inibição da Hemaglutinação , Hemaglutinação por Vírus/imunologia , Humanos , Vírus da Influenza A Subtipo H1N1/crescimento & desenvolvimento , Vírus da Influenza A Subtipo H1N1/imunologia , Vírus da Influenza A Subtipo H1N1/isolamento & purificação , Vírus da Influenza A Subtipo H1N1/patogenicidade , Influenza Humana/imunologia , Influenza Humana/virologia , Especificidade de Órgãos/imunologia , Pandemias , Ratos , Federação Russa/epidemiologia , Suínos
2.
Ukr Biokhim Zh ; 47(5): 619-34, 1975.
Artigo em Russo | MEDLINE | ID: mdl-128174

RESUMO

A study in the enzymatic properties of muscle membranes established that sarcolemma of the rabbit skeletal muscles contains the Ca2+-ATPase system which does not require Mg2+ for manifestation of ions activity. By some kinetic properties it differs from ATPase of myosin. The complex Ca-ATP2+ is a substrate of Ca2+-ATPase. Ions of a series of bivalent metals inhibit the latter as well as the passive transport of Ca2+, that may evidence for a definite relation of Ca2+-ATPase with Ca+2 transport in skeletal muscles. Acetyl cholinesterase and AMP-aminohydrolase are strongly bound with the sarcolemma. The sarcolemma structural organization is shown to play a certain role in manifestation of their activity. On the basis of the data obtained when studying the activity in the ATPase systems and dynamics of formation and decay of the intermediate phosphorylated product in the microsomal fraction of cow and rabbit myometrium certain peculiarities are established for the active mechanisms of Ca2+ transport in smooth muscles. A problem is under discussion on the possible active participation of sarcolemma in regulation of Ca2+ concentration in the smooth muscle cells. Two ATPase systems, Mg2+-dependent and Mg2+-dependent Ca2+ activated are found in nuclei; the role of lipids of the skeletal muscles in manifestation of their activity is studied. AMP-amino hydrolase properties are characterized for different areas of the sarcoplasmatic reticulum membranes. The model of E-avitaminous muscular distrophy was used to show disturbances in the structure of sarcolemma and membranes of the sarcoplasmatic reticulum which are accompanied by changes in their ATPase and Ca2+-transporting properties.


Assuntos
Adenosina Trifosfatases/metabolismo , Músculos/enzimologia , Sarcolema/enzimologia , Animais , Cálcio/farmacologia , Membrana Celular/enzimologia , Ativação Enzimática/efeitos dos fármacos , Magnésio/farmacologia , Distrofia Muscular Animal/enzimologia , Coelhos , Sarcolema/efeitos dos fármacos , Retículo Sarcoplasmático/efeitos dos fármacos , Retículo Sarcoplasmático/enzimologia , Deficiência de Vitamina E/enzimologia
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