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1

Serum proteins in stray dogs using high-resolution electrophoresis

100%
Czernomysy-Furowicz D., Karakulska J., Nowak M., Mazur J.
Advances in Agricultural Sciences
|
2004
|
tom 09
2

Changes in the content of major proteins and selected hormones in the blood serum of piglets during the early postnatal period

72%
Szymeczko R., Kapelanski W., Piotrowska A., Dybala J., Boguslawska-Tryk M., Burlikowska K., Hertig I., Sassek M., Pruszynska-Oszmalek E., Mackowiak P.
Folia Biologica
|
2009
|
tom 57
|
nr 1-2
97-103
3

Effect of pretreatment of wells in polystyrene plates on adsorption of some human serum proteins

72%
Kochanowska I. E., Rapak A., Szewczuk A.
Archivum Immunologiae et Therapiae Experimentalis
|
1994
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tom 42
|
nr 2
4

Nuclear localization and binding affinity of STAT5b for the alpha2-macroglobulin gene promoter during rat liver development and the acute-phase response

72%
Mihailovic M., Dinic S., Bogojevic D., Ivanovic-Matic S., Uskokovic A., Arambasic J., Grigorov I., Grdovic N., Vidakovic M., Martinovic V., Petrovic M., Poznanovic G.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr 2
Expression of the rat α2-macroglobulin (MG) gene undergoes dynamic changes throughout an individual's life and during the acute-phase (AP) response. Details of the participation of the STAT family of transcription factors in its control remain incompletely understood. Here we examined the involvement of STAT5b in MG gene expression during development and the AP response. Immuno-blot analysis revealed the highest nuclear level of STAT5b in the fetus and during postnatal development, whereas in the adult it decreased. Stimulation of MG expression during the AP response was accompanied by a decrease in STAT5b. Examination of STAT5b localization revealed that the relative concentrations of STAT5b were higher in the nuclear matrix than in the nuclear extract. Affinity chromatography with the extended promoter region of the MG gene (-825/+12), followed by immuno-blot analysis, revealed dynamic changes in STAT5b binding. The highest concentration of the promoter-binding form of STAT5b was observed in the fetus. As postnatal development progressed, the level of promoter-bound STAT5b decreased and in the adult liver it was the lowest. Stimulation of MG gene expression during the AP response in both the fetus and adult was accompanied by significantly decreased STAT5b binding to the MG promoter. The AP response was accompanied by lower levels of STAT5b serine and tyrosine phosphorylation in both fetus and adult. In the nuclear matrix derived from adult tissues, tyrosine phosphorylated species were completely absent. We conclude that developmental-stage differences in the mechanisms that determine STAT5b nuclear localization contribute to its activity in vivo.
5

Antigenic marker of beta-macroglobulins in sheep-epitope Ns 1

72%
Skiba E., Wegrzyn J.
Roczniki Naukowe Zootechniki
|
1999
|
tom 26
|
nr 4
6

Supramolecularity creates nonstandard protein ligands

72%
Piekarska B., Rybarska J., Stopa B., Zemanek G., Krol M., Roterman I., Konieczny L.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 4
Congo red and a group of structurally related dyes long used to stain amyloid proteins are known to associate in water solutions. The self-association of some dyes belonging to this group appears particularly strong. In water solutions their molecules are arranged in ribbon-like micellar forms with liquid crystalline properties. These compounds have recently been found to form complexeswith some native proteins in a non-standard way. Gaps formed by the local distribution of β-sheets in proteins probably represent the receptor sites for these dye ligands. They may result from higher structural instability in unfolding conditions, but also may appear as long range cooperative fluctuations generated by ligand binding. Immunoglobulins G were chosen as model binding proteins to check the mechanism of binding of these dyes. The sites of structural changes generated by antigen binding in antibodies, believed to act as a signal propagated to distant parts of the molecule, were assumed to be suitable sites for the complexation of liquid-crystalline dyes. This assumption was confirmed by proving that antibodies engaged in immune complexation really do bind these dyes; as expected, this binding affects their function by significantly enhancing antigen binding and simultaneously inhibiting C1q attachment. Binding of these supramolecular dyes by some other native proteins including serpins and their natural complexes was also shown. The strict dependence of the ligation properties on strong self-assembling and the particular arrangement of dye molecules indicate that supramolecularity is the feature that creates non-standard protein ligands, with potential uses in medicine and experimental science.
7

Crystal structure of rat transthyretin at 2.5 A resolution: First report on a unique tetrameric structure

72%
Wojtczak A.
Acta Biochimica Polonica
|
1997
|
tom 44
|
nr 3
The first observation of a unique tetrameric molecular structure of transthyretin from rat (rlTR, prealbumin) is reported. The structure has been determined by X-ray diffraction using molecular replacement and the structure of human transthyretin (hTTR) as a starting model. Crystals of native rat transthyretin are tetragonal, space group P4 3 2 1 2, and have four independent monomers in the asymmetric unit of the crystal lattice. Data were collected to 2.5 A resolution and the structure has been refined to R = 18.9% for 13584 data points between 6-2.5 A resolution. Like hTTR, the rat protein is also a 54000 Da tetramer with four identical polypeptide chains of 127 amino-acid residues. Of the 22 amino-acid residues which are different in the human and rat TTR sequences, none are in the thyroxine binding domain. Analysis of these data reveal that the tertiary structure of rTTR is similar to that of hTTR with only small differences in the flexible loop regions on the surface of the protein. As a result of local changes in flexible loop regions near residues 30-41, 60-65 and 102-104, the structure of rTTR monomers is more compact than that of the corresponding hTTR monomers. The loop between residues 30-41 is bound closer to the monomer core in the former as compared with the latter structure and there is a wider opening of the space formed between these loops at two adjacent monomeric subunits. These conformational changes do not affect the interfaces between the monomeric subunits and are not transmitted to the thyroxine binding site so that its topology remains not altered.
8
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The detection of specific acute phase serum protein complexes and immune complexes by Congo Red binding

72%
Rybarska J., Konieczny L., Piekarska B., Stopa B., Roterman I.
Journal of Physiology and Pharmacology
|
1995
|
tom 46
|
nr 2
9

Serum protein fractions in healthy sows during perinatal period

58%
Fijalkowski K., Silecka A., Czernomysy-Furowicz D.
Advances in Agricultural Sciences
|
2011
|
tom 14
|
nr 1-2
10

Changes in blood chemistry in broiler chickens during the fattening period

58%
Piotrowska A., Burlikowska K., Szymeczko R.
Folia Biologica
|
2011
|
tom 59
|
nr 3-4
11

Abnormalities in serum proteins in the course of babesiosis in dogs

58%
Zygner W., Gojska-Zygner O., Wedrychowicz H.
Bulletin of the Veterinary Institute in Puławy
|
2011
|
tom 55
|
nr 1
The objectives of this study were to evaluate the serum protein electrophoresis pattern in dogs infected with B. canis, and correlation between haematocrit and albumin/globulin ratio. The infection with B. canis was confirmed by PCR and sequencing of PCR products. Total serum protein concentrations were determined by a clinical chemistry analyser. Albumin, α₁-, α₂-, β₁-, β₂-, and γ-globulin concentrations were assayed by densitometric analysis after electrophoretic separation of serum proteins on agarose gel. The most common disorders in affected dogs were decreased α-globulin fractions, increased ß-globulin concentration, increased albumin/globulin (A/G) ratio, and hypoglobulinaemia. A decrease in ar and α₂-globulin concentration was detected accordingly in 54.8% and 32.3% of dogs. An increase in β₁- and β₂-globulin concentration, and increased A/G ratio was detected accordingly in 38.7%, 51.6%, and 38.7% of dogs. Hypoglobulinaemia was detected in 32.3% dogs. Changes detected in this study probably result from haemolysis, hypertransferrinaemia, increased C3a protein concentration (complement), and dehydration.
12

Conglutinin, CL-43 and CL-46 - three bovine collectins

58%
Dec M., Wernicki A.
Polish Journal of Veterinary Sciences
|
2006
|
tom 09
|
nr 4
Conglutinin, collectin-43 (CL-43) and collectin-46 (CL-46) are serum proteins characteristic for Bovidae. They belong to collectins - family of oligomeric proteins composed of trimeric subunits containing collagen-like sequences joined to C-type lectin domains. The genes encoding conglutinin, CL-43 and CL-46 are located on the bovine chromosome 28, and phylogenetic analysis indicates their common origin - from the lung surfactant protein D gene. Northern blot or immunocytochemical analysis confirm biosynthesis of bovine collectins mainly in the liver (conglutinin, CL-43) and in the thymus (CL-46). The level of conglutinin in the serum of dairy cows depends on many factors such as breeding, the season of the year, the stage of the reproductive cycle and infection. The collectins are involved in the innate immune defense. They bind to microbial surface carbohydrates inducing aggregation and, thereby, impeding infectivity. On the other hand the destruction of pathogens occurs due to stimulation of effector cells. CL-43 as well as conglutinin, binds to the collectin receptor (ClqR) localized on many types of cells identified as a surface variant of calreticulin. Conglutinin and CL-43 show antiviral activities towards influenza A virus and rotaviruses. Conglutinin also displays protective activity against bacterial infections.
13

Genetic characteristics of Mouton Charollais sheep bred in Poland and their crossbreds with Polish Merino

58%
Rychlik T., Duniec M. J.
Roczniki Naukowe Zootechniki
|
1999
|
tom 26
|
nr 4
14

Effect of deltamethrin on serum proteins and IgG and IgM concentrations in mice

58%
Lukowicz-Ratajczak J., Krechniak J.
Acta Poloniae Toxicologica
|
1995
|
tom 03
|
nr 1
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