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1.
Dokl Biol Sci ; 502(1): 26-30, 2022 Jun.
Article in English | MEDLINE | ID: mdl-35298750

ABSTRACT

The article presents a report on the findings of representatives of frenulate pogonophorans Nereilinum murmanicum in the northern and central parts of the Barents Sea, which significantly expands the range of this species and provides guidance on its distribution in this basin. Here we present the coordinates of new finds with an indication of the depth. Find points were associated with data on known and potential hydrocarbon deposits.


Subject(s)
Annelida , Polychaeta , Animals , Hydrocarbons
2.
Urologiia ; (4): 97-99, 2016 Aug.
Article in Russian | MEDLINE | ID: mdl-28247734

ABSTRACT

The annual number of cases of kidney transplantation in the Russian Federation varies from 900 to 1000. The generally accepted method of operation is the heterotopic allotransplantation into one of the iliac region. Proper kidney recipient are psychologically "forgotten", often completely lost sight of postoperative monitoring, especially in the long term, but may remind of itself in extraordinary cases like ours.


Subject(s)
Carcinoma, Renal Cell/pathology , Kidney Neoplasms/pathology , Kidney Transplantation , Kidney/pathology , Postoperative Complications/diagnosis , Adult , Carcinoma, Renal Cell/therapy , Humans , Kidney Neoplasms/therapy , Male , Postoperative Complications/pathology , Transplantation, Heterotopic
4.
FEBS Lett ; 290(1-2): 95-8, 1991 Sep 23.
Article in English | MEDLINE | ID: mdl-1915899

ABSTRACT

FPLC separation of alpha- and beta-subunits of phenylalanyl-tRNA synthetases from E. coli MRE-600 and Thermus thermophilus HB8 has been carried out in the presence of urea. Native alpha-subunits of both enzymes were primarily alpha 2-dimers and tended to aggregate. Most E. coli enzyme beta-subunits were monomeric and only a small fraction was represented by beta 2-dimers. All thermophilic beta-subunits were beta 2-dimers. It was shown that monomers and all forms of homologous subunits had no catalytic activity in tRNA(Phe) aminoacylation. For the enzymes and their subunits, titration curves were obtained and isoelectric points were determined. The comparison of the relative surface charges indicated similarity of the surfaces of entire enzymes and the corresponding beta-subunits. Alpha-subunits displayed a distinctly different pH dependence of the surface charge. A spatial model of the oligomeric structure and a putative mechanism for its formation are discussed.


Subject(s)
Escherichia coli/enzymology , Phenylalanine-tRNA Ligase/chemistry , Thermus thermophilus/enzymology , Chromatography , Electrophoresis, Polyacrylamide Gel , Hydrogen-Ion Concentration , Isoelectric Point , Macromolecular Substances , Molecular Structure , Molecular Weight
5.
Mol Biol (Mosk) ; 24(3): 788-94, 1990.
Article in Russian | MEDLINE | ID: mdl-2205792

ABSTRACT

A rapid and efficient procedure for isolating homogeneous beef liver phenylalanyl-tRNA synthetase (EC.6.1.1) was developed that enables to purify the enzyme 5000 fold and to achieve the activity of 8 e.a.u. per mg of protein. The molecular mass of the native enzyme was estimated to be 260 kDa, for alpha subunit - 59 kDa, and for beta - 72 kDa. Two cellular clones were derived by means of hybridization of immunised splenocytes with myeloma cells. They secrete monoclonal antibodies, designated P6 and P1 2, that bind to human placental and bovine liver phenylalanyl-tRNA synthetases but not to the same enzymes from E. coli and T. thermophilus. P6 and P1 2 antibodies do not affect the aminoacylation capacity of human or bovine phenylalanyl-tRNA synthetases. By immunoblotting, it was shown that P6 antibodies recognize the alpha subunit of the enzyme.


Subject(s)
Amino Acyl-tRNA Synthetases/isolation & purification , Antibodies, Monoclonal/isolation & purification , Liver/enzymology , Phenylalanine-tRNA Ligase/isolation & purification , Animals , Cattle , Escherichia coli/enzymology , Humans , Immunoblotting , Immunohistochemistry , Molecular Weight , Phenylalanine-tRNA Ligase/immunology , Species Specificity , Thermus/enzymology
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