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1
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Sedimentation of water dispersed systems of acrylate copolymers in xylene

100%
Makarewicz E., Zalewska A.
Polish Journal of Chemical Technology
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2008
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vol. 10
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issue 3
29-34
EN
Methyl methacrylate - butyl acrylate - methacrylic acid copolymer and butyl methacrylate - methacrylic acid amide copolymer of a different segmental structure were stabilised with non-ionic and anionic surfactants. Gel chromatography, viscosimetry, tensiometry, conductometry and sedimentation methods were applied to define the properties of the synthesized copolymers, surfactants in water solutions and water dispersions. The types and the properties of the phases being in a state of sedimentation balance were also determined. The obtained experimental data were interpreted and justified by using the copolymer and surfactants properties. The existing correlations were pointed out. The obtained results show that the stability of a disperse system considerably depends on the structure of the copolymer. The MMA/BA/MAA copolymer has monomeric units of elastic butyl acrylate. Segments containing these monomeric units adsorb surfactants much better and form more stable water disperse systems. However, the MBA/AMAA copolymer with the polarity of amide group of methacrylamide makes disperse systems less stable.
2
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Structure and biosynthesis of human salivary mucins.

81%
Zalewska A., Zwierz K., Żółkowski K., Gindzieński A.
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2000
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vol. 47
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issue 4
1067-1079
EN
Human salivary glands secrete two types of mucins: oligomeric mucin (MG1) with molecular mass above 1 MDa and monomeric mucin (MG2) with molecular mass of 200-250 kDa. Monomers of MG1 and MG2 contain havily O-glycosylated tandem repeats located at the central domain of the molecules. MG1 monomers are linked by disulfide bonds located at sparsely glycosylated N- and C-end. MG1 are synthesized by mucous cells and MG2 by the serous cells of human salivary glands.
3
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Determination of lysosomal exoglycosidases in human saliva

61%
Chojnowska S., Zalewska A., Knaś M., Waszkiewicz N., Waszkiel D., Kossakowska A., Zwierz K.
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2014
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vol. 61
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issue 1
85-90
EN
Background: Currently we observe a growing interest in human saliva as a non-invasive material for diagnosis and monitoring of general and oral diseases. Methods: The aim of our study was adaptation of the Marciniak et al. (Marciniak J, Zalewska A, Popko J, Zwierz K, 2006, Clin Chem Lab Med 44: 933-937) method for determination of HEX and GLU activity in synovial fluid, and for determination of: HEX and GLU, as well as MAN, GAL, and FUC activity in human saliva. Results: Under optimal conditions, 10 μl of saliva for HEX, and 30 μl for GLU, MAN, GAL and FUC, were sufficient for determination of human salivary exoglycosidases activity with variation coefficient ranging from 0.89 for GLU to 0.99 for GAL. Conclusion: The adapted method for exoglycosidases activity determination in human saliva is sufficiently sensitive and precise to use in clinical diagnosis.
4
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Activity of lysosomal exoglycosidases in submandibular glands of rats intoxicated by cadmium at doses related to human chronic environmental and occupational exposures.

61%
Zalewska A., ska M. M. B., Marciniak J., Karaszewska K., Zwierz K., Moniuszko-Jakoniuk J.
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vol. 51
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issue 3
831-837
EN
Work in cadmium (Cd) smelter and smoking cigarettes damages teeth and oral mucosa which are protected by tissue and salivary glycoconjugates: glycoproteins, glycolipids, and proteoglycans. We worked out a rat model imitating human "environmental" and "occupational" exposure to cadmium using 5 mg Cd and 50 mg Cd/l in drinking water, respectively. In submandibulary glands of exposed to Cd rats, we found the time and dose dependent accumulation of Cd and simultanous decrease in activity of β-N-acetylhexosaminidase (HEX). In homogenates of submandibulary glands of control rats, β-N-acetylhexosaminidase showed the highest activity. The activities of α;-mannosidase and β-galactosidase were very low. None of these exoglycosidases were inhibited by Cd even at 44 mM concentration.
5
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Isoenzymes of N- acetyl-β-hexosaminidase

51%
Zwierz K., Zalewska A., Zoch-Zwierz W.
Acta Biochimica Polonica
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1999
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vol. 46
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issue 3
739-751
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