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1

Azurocidin - inactive serine proteinase homolog acting as a multifunctional inflammatory mediator

100%
Watorek W.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr 3
Azurocidin, also known as cationic antimicrobial protein 37 kDa (CAP37) or hepa­rin-binding protein (HBP) is an inactive homolog of serine proteinases residing in granulocytes. The ability to cleave peptide bond was lost due to replacement of two of the three residues from the conserved catalytic triad characteristic for serine protein- ases. Azurocidin has a broad spectrum of antimicrobial activity, mainly against Gram-negative bacteria. It is also recognized as a multifunctional inflammatory medi­ator for its contracting effects on endothelial cells causing an increase of vascular per­meability, capacity to bind endotoxin and ability to attract monocytes to inflammation sites.
2

Ultrastructural localization of acid phosphatase in Rhodotorala glutinis

88%
Watorek W.
Acta Microbiologica Polonica
|
1983
|
tom 32
|
nr 3
3

Acid phosphatase relased to the growth medium by Rhodotorula glutinis. Purification and some properties of the enzyme

63%
Watorek W., Kwiatkowska G.
Acta Microbiologica Polonica
|
1983
|
tom 32
|
nr 3
4

Acid phosphatase of the yeast Saccharomyces cerevisiae. Purification and properties of the enzyme

63%
Watorek W., Morawiecka B.
Acta Societatis Botanicorum Poloniae
|
1977
|
tom 46
|
nr 2
5

Acid phosphatase secreted by roots of yellow lupine (Lupinus luteus)

63%
Golen A., Watorek W.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
6

Function of carbohydrate moiety in acid phosphates of Rhodotorula glutinis

63%
Watorek W., Morawiecka B.
Acta Biochimica Polonica
|
1984
|
tom 31
|
nr 2
7

The 35 kDa acid phosphatase isolated from lupin (Lupinus luteus) cotyledons displaying characteristics of LMW tartrate resistant acid phosphatases (TRAP)

51%
Szalewicz A., Rzodeczko H., Dudek P., Watorek W.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr Supplement 4
8

Phosphodiesterase activity in the vegetative organs of the yellow lupin (Lupinus luteus)

51%
Szalewicz A., Brzuszkiewicz A., Watorek W.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
9

Cloning, expression and purification of serprocidins in Pichia pastoris

51%
Indyk K., Wezyk P., Watorek W., Olczak M.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr Supplement 1
10

Comparative analysis of avian and reptilian egg white proteins

51%
Ciuraszkiewicz J., Olczak M., Watorek W.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
11

Acid phosphatase of the yeast Rhodotorula rubra. Purification and properties of the enzyme

51%
Watorek W., Morawiecka B., Korczak B.
Acta Biochimica Polonica
|
1977
|
tom 24
|
nr 2
12

Plant purple acid phosphatases - genes, structures and biological function

51%
Olczak M., Morawiecka B., Watorek W.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr 4
The properties of plant purple acid phosphatases (PAPs), metallophosphoesterases present in some bacteria, plants and animals are reviewed. All members of this group contain a characteristic set of seven amino-acid residues involved in metal li- gation. Animal PAPs contain a binuclear metallic center composed of two irons, whereas in plant PAPs one iron ion is joined by zinc or manganese ion. Among plant PAPs two groups can be distinguished: small PAPs, monomeric proteins with molecular mass around 35 kDa, structurally close to mammalian PAPs, and large PAPs, homodimeric proteins with a single polypeptide of about 55 kDa. Large plant PAPs exhibit two types of structural organization. One type comprises enzymes with subunits bound by a disulfide bridge formed by cysteines located in the C-terminal region around position 350. In the second type no cysteines are located in this posi­tion and no disulfide bridges are formed between subunits. Differences in structural organisation are reflected in substrate preferences. Recent data reveal in plants the occurrence of metallophosphoesterases structurally different from small or large PAPs but with metal-ligating sequences characteristic for PAPs and expressing pro­nounced specificity towards phytate or diphosphate nucleosides and inorganic pyrophosphate.
13

The use of sequential affinity chromatography for separation of human neutrophil elastase, cathepsin G and azurocidin

51%
Watorek W., Polanowski A., Wilusz T.
Acta Biochimica Polonica
|
1996
|
tom 43
|
nr 3
Elastase, cathepsin G and azurocidin from human neutrophils are key components of body inflammatory defense. Perturbations in regulation of their activities lead to many serious pathological states. The paper describes a simple, fast and efficient method of joint purification of these proteins with the use of sequential affinity chromatography on squash trypsin inhibitor (CMTI I) and bovine pancreatic trypsin inhibitor (BPTI).
14

Isolation and characterisation of crocodile and python ovotransferrins

51%
Ciuraszkiewicz J., Olczak M., Watorek W.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr 1
Transferrins play a major role in iron homeostasis and metabolism. In vertebrates, these proteins are synthesised in the liver and dispersed within the organism by the bloodstream. In oviparous vertebrates additional expression is observed in the oviduct and the synthesised protein is deposited in egg white as ovotransferrin. Most research on ovotransferrin has been performed on the chicken protein. There is a limited amount of information on other bird transferrins, and until our previous paper on red-eared turtle protein there was no data on the isolation, sequencing and biochemical properties of reptilian ovotransferrins. Recently our laboratory deposited ten new sequences of reptilian transferrins in the EMBL database. A comparative analysis of these sequences indicates a possibility of different mechanisms of iron release among crocodile and snake transferrin. In the present paper we follow with the purification and analysis of the basic biochemical properties of two crocodile (Crocodilus niloticus, C. rhombifer) and one snake (Python molurus bivittatus) ovotransferrins. The proteins were purified by anion exchange and hydrophobic chromatography, and their N-terminal amino-acid sequences, molecular mass and isoelectric points were determined. All three proteins are glycosylated and their N-glycan chromatographic profiles show the largest contribution of neutral oligosaccharides in crocodile and disialylated glycans in python ovotransferrin. The absorption spectra of iron-saturated transferrins were analysed. Iron release from these proteins is pH-dependent, showing a biphasic character in crocodile ovotransferrins and a monophasic type in the python protein. The reason for the different types of iron release is discussed.
15

Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity

45%
Indyk K., Olczak T., Ciuraszkiewicz J., Watorek W., Olczak M.
Acta Biochimica Polonica
|
2007
|
tom 54
|
nr 3
Azurocidin is an inactive serine protease homolog with primary sequence similarity to neutrophil elastase, cathepsin G, and proteinase 3. The aim of this study was to investigate possible consequences of differential glycosylation of azurocidin in regard to its secretion, protein stability as measured by susceptibility to proteolysis, and antibacterial activity. Site-directed mutagenesis was employed to generate mutant azurocidin variants lacking individual N-glycosylation sites. Our results show that N-linked glycans may play a role in proper azurocidin folding and subsequent secretion by insect cells. We also demonstrate that N-linked glycosylation contributes to azurocidin stability by protecting it from proteolysis. The lack of N-glycosylation at individual sites does not significantly influence the azurocidin antibacterial activity.
16

Drobnoustroje w biologicznej ochronie roślin przed chorobami grzybowymi

39%
Grzegorczyk M., Szalewicz A., Zarowska B., Polomska X., Watorek W., Wojtatowicz M.
Acta Scientiarum Polonorum. Biotechnologia
|
2015
|
tom 14
|
nr 2
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