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1

Enhanced vigilin and anionic trypsinogen expression in experimental chronic pancreatitis

100%

Hilgendorf I., Aßmuth K., Sparmann G., Emmrich J., Kruse C.

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EN

The molecular principles that lead to chronic pancreatitis are incompletely understood. Trypsin(ogen) plays a key role in the development of pancreatitis. Since the production of trypsin(ogen) by acinary pancreatic cells is paralleled by the expression of vigilin we hypothesised that vigilin may be involved in the onset of pancreatitis. Vigilin is a ubiquitous protein and has apparently high affinity to RNA. In the present study experimental pancreatitis was induced in male rats by a single intravenous application of dibutyltin dichloride (DBTC). Sections of rat pancreas were immunostained with an affinity-purified polyclonal antiserum against vigilin or trypsin(ogen). The changes in vigilin and trypsin(ogen) protein expression were determined by immunoblotting and subsequent sequence analysis of the amino acids. Induction of pancreatitis by DBTC caused alterations in the distribution and the amount of both vigilin and trypsin(ogen) as shown by immunohistochemical and immunoblot analysis. Furthermore we could demonstrate that anionic trypsinogen expression is up-regulated in DBTC-induced chronic pancreatitis. The obtained results suggest that vigilin as well as trypsin(ogen) are involved in the pathogenesis of pancreatitis and that the long-time DBTC-induced pancreatitis is a useful model for study of chronic pancreatitis.

2

Selective adsorption of trypsin using molecularly imprinted polymers prepared with PEG-based hydrogels containing anionic functional monomers

100%

Kubo T., Arimura S., Naito T., Otsuka K.

Molecular Imprinting

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2014

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vol. 2

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issue 1

EN

Molecularly imprinting (MI) hydrogels for selective adsorption of trypsin are reported. The trypsin imprinted hydrogels were prepared using a polyethylene glycol (PEG)-based dimethacrylate as a crosslinker and anionic functional monomers. The hydrogel prepared without any functional monomers showed significantly low ability to adsorb a variety of proteins. We optimized the concentration and the length of PEG units of the crosslinkers to achieve the complete removal of the template molecule and suitable selective adsorption. Additionally, the functional monomers chosen were anionic since the template, trypsin, is a basic protein. The adsorption tests for proteins, done on the prepared MI gels, indicated that the MI gel prepared with sodium allyl sulfonate (AS) as a functional monomer showed much higher selective adsorption for trypsin, even though a mixture of trypsin and cytochrome c was used as the protein solution. The selective adsorption was more effective in a NaCl solution in which the non-specific adsorption by a sulfonate is suppressed, similarly to our findings in a previous study. The MI gel prepared with acrylic acid also showed the selectivity, although the adsorption strength was lower than that of the MI gel containing AS. We believe that the present study constitutes the first approach for the selective adsorption of trypsin using PEG-based hydrogels.

3

Effects of specific inhibitors on the gene expression of a digestive trypsin in Pieris brassicae L. (Lepidoptera: Pieridae)

88%

Sendi J. J., Ali S., Arash Z., Talebi J. K.

Journal of Plant Protection Research

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2018

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vol. 58

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issue 1

4

Trypsin-specific Inhibitors from the Macrolepiota procera, Armillaria mellea and Amanita phalloides wild mushrooms

75%

Lukanc T., Brzin J., Kos J., Sabotič J.

Acta Biochimica Polonica

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2017

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vol. 64

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issue 1

21-24

EN

Wild growing mushrooms are a rich source of novel proteins with unique features. We have isolated and characterized trypsin inhibitors from two edible mushrooms, the honey fungus (Armillaria mellea) and the parasol mushroom (Macrolepiota procera), and from the poisonous death cap (Amanita phalloides). The trypsin inhibitors isolated: armespin, macrospin and amphaspin, have similar molecular masses, acidic isoelectric points and are not N-glycosylated. They are very strong trypsin inhibitors and weak chymotrypsin inhibitors. They are resistant to exposure to high temperatures and withstand extreme pH values. These exceptional characteristics are advantageous for their potential use in biotechnology, agriculture and medicine.

5

Spectroscopic methods of studying enzyme action in wool fibre

63%

Fogorasi M., Heine E.

Open Chemistry

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2006

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vol. 4

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issue 4

786-797

EN

Enzymes may be used to develop an environmentally friendly alternative to the conventional polluting technologies in textile finishing. The action of the unlabeled and fluorescent labeled proteolytic enzymes subtilisin and trypsin on wool was examined. Scanning electron micrographs and a diffusion study, based on fluorescence microscopy, localized the enzymatic attack on the fiber. A kinetic study was carried out by monitoring the amino acid content of the treatment liquor. Enzymatic action is not confined to the fiber surface. To limit attack to the surface and reduce wool damage new treatment methods such as enzyme immobilization onto a solid carrier must be investigated.

6

Non-conventional affinity chromatography of serine proteinases and their inhibitors.

63%

Polanowski A., Wilimowska-Pelc A., Kowalska J., Grybel J., Żelazko M., Wilusz T.

Acta Biochimica Polonica

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2003

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vol. 50

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issue 3

765-773

EN

From among a wide variety of protein purification techniques affinity chromatography has proved to be particularly effective for separation of proteolytic enzymes and their inhibitors. In this article, following a general description of affinity adsorbents used for purification of proteinases, we overview a simple separation procedure for some serine proteinases and their inhibitors by way of affinity chromatography in the presence of high NaCl concentration. It has been shown that some highly specific trypsin inhibitors exhibit also antichymotrypsin activity when high concentration of Na+ but not K+ or Li+ ions are present in the reaction mixture. Taking advantage of this phenomenon the virgin forms of trypsin inhibitors from squash seeds, Kazal-type inhibitor from porcine pancreas and α1-proteinase inhibitor from human and sheep plasma, as an example, were separated using immobilized chymotrypsin or its inactive derivative methylchymotrypsin in the presence of 5 M NaCl.

Refine search results

Enhanced vigilin and anionic trypsinogen expression in experimental chronic pancreatitis

Selective adsorption of trypsin using molecularly imprinted polymers prepared with PEG-based hydrogels containing anionic functional monomers

Effects of specific inhibitors on the gene expression of a digestive trypsin in Pieris brassicae L. (Lepidoptera: Pieridae)

Trypsin-specific Inhibitors from the Macrolepiota procera, Armillaria mellea and Amanita phalloides wild mushrooms

Spectroscopic methods of studying enzyme action in wool fibre

Non-conventional affinity chromatography of serine proteinases and their inhibitors.