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Elektroforetyczna identyfikacja proteinaz cysteinowych w surowicach pacjentów z przewlekłą białaczką limfocytową (PBL) z wykorzystaniem biotynylowanego jodoacetamidu

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Młudzik P. , Pietrzak J. , Saed L. , Wodziński D. , Franiak–Pietryga I. , Mirowski M.

Folia Medica Lodziensia

2016

tom 43

nr 1

35-55

Introduction: Cysteine proteases are enzymes that regulate numerous physiological and pathological processes in the human body. Disorders of their activity can lead to a number of diseases. They play an important role in the process of carcinogenesis, participating in the invasion, transformation, angiogenesis, apoptosis and metastasis. The aim of this study was to elaborate the electrophoretic method of cysteine proteinases identification in the sera of patients suffering from chronic lymphocytic leukemia based on biotinylated iodoacetamide. Material and methods: Preliminary studies were carried out on the commercially available papain (EC 3.4.22.2) well known and widely used plant cysteine protease with a molecular weight 23,4 kDa. The study was conducted on the blood samples taken from patients with chronic lymphocytic leukemia (CLL) and control sera from healthy donors. The sera after the preincubation with iodoacetamide were mixed with the sample buffer followed by electrophoresis on polyacrylamide gel containing sodium dodecyl sulfate (SDS–PAGE). The separated proteins were electrophoretically transferred to the nitrocellulose membranes and subjected to the further analysis using streptavidin conjugated with horseradish peroxidase (HRP). The use of substrate for HRP 3,3’- diaminobenzidine tetrachloride (DAB) allows the biotinylated iodoacetamide and thereby cysteine proteinase identification. Results: The comparative analysis of the sera from the patients with chronic lymphocytic leukemia and the control sera led to the identification of additional protein with a cysteine protease characteristic having a molecular weight of about 37 kDa, which did not occur or was present in a smaller amount of the control sera. Conclusions: The developed method allows the detection of cysteine proteases which are present in the control sera and the sera of patients with chronic lymphocytic leukemia.

Roles of endogenous prostaglandins and cyclooxygenase isozymes in mucosal defense of inflamed rat stomach

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Takeeda M. , Hayashi Y. , Yamato M. , Murakami M. , Takeuchi K.

Journal of Physiology and Pharmacology

2004

tom 55

nr 1,2

Endogenous prostaglandins (PGs) are involved in adaptive gastric protection against acute injury, and cyclooxygenase (COX)-1 is responsible for the production of PGs in this phenomenon. In the present study, we examined the effect of various COX inhibitors on gastric ulcerogenic and acid secretory responses following daily exposure of the stomach to iodoacetamide (IA) and investigated the role for COX isozyme in gastric protection under subchronic mucosal irritation. Gastric mucosal irritation was induced by addition of 0.1% IA to drinking water, and the gastric mucosa was examined on the 6th day. Indomethacin (5 mg/kg) or SC-560 (selective COX-1 inhibitor, 5 mg/kg) or rofecoxib (selective COX-2 inhibitor, 5 mg/kg) was given p.o. twice 24 hr and 3 hr before the termination of IA treatment. Giving IA in drinking water for 5 days produced minimal damage in the stomach. The damage was significantly worsened by indomethacin, resulting in hemorrhagic lesions. Both SC-560 and rofecoxib also aggravated such lesions, although the effect of rofecoxib was more pronounced. Treatment with IA decreased acid secretion in pylorus-ligated stomachs, and this change was significantly reverted by indomethacin as well as SC-560 and rofecoxib. Mucosal PGE2 content was increased following IA treatment, with apparent expression of COX-2 mRNA in the stomach, and the increased PGE2 production was significantly suppressed by SC-560 and rofecoxib as well as indomethacin. These results suggest that endogenous PGs derived from both COX-1 and COX-2 are involved in the mucosal defense of the inflamed stomach, partly by decreasing acid secretion and contribute to maintaining the mucosal integrity under such conditions.

Two disulphide bridges are present in juvenile hormone binding protein from Galleria mellonella

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Kolodziejczyk R. , Dobryszycki P. , Ozyhar A. , Kochman M.

Acta Biochimica Polonica

2001

tom 48

nr 4

The hemolymph juvenile hormone binding protein (JHBP) from Galleria mellonella contains two disulphide bridges/molecule and no free Cys residues. An alignment of primary structures of other Lepidopteran JHBPs indicates that Cys residues, equivalent to Cys10,17,151,195 in G. mellonella JHBP, may be involved in -S-S- bridge formation.