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1

Comparison of specificity of human and horse leucocyte proteinases with synthetic peptide substrates

100%
Dubin A., Potempa J., Schnebli H. P., Koj A.
Folia Histochemica et Cytobiologica
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1986
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tom 24
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nr 2
2

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

100%
Watorek W., Polanowski A., Wilusz T.
Acta Biochimica Polonica
|
1996
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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).
3

Was the serine protease cathepsin G discovered by S. G. Hedin in 1903 in bovine spleen?

84%
Palesch D., Sienczyk M., Oleksyszyn J., Reich M., Wieczerzak E., Boehm B., Burster T.
Acta Biochimica Polonica
|
2011
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tom 58
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nr 1
 In the beginning of the 20th century, enzymes with proteolytic activity were classified as peptidases, Erepsin, and proteases. Among these, pepsin, trypsin, and autolytic enzymes were of the protease class. Spleen-derived proteases were poorly characterized until Sven Gustaf Hedin performed several digestion experiments with bovine spleen. He incubated minced bovine spleen under acidic or neutral conditions and characterized two active proteases; the results were published in 1903. The first protease was named α-protease and was active under neutral conditions. The second was named β-protease and was active under acidic conditions. We replicated Hedin's experiments according to his methods and found, by using activity-based probes to visualize proteases, that the historical α-protease is the present-day serine protease cathepsin G (CatG), which is known to be important in several immune processes, including antigen processing, chemotaxis, and activation of surface receptors. The β-protease, however, comprised different proteases including CatX, B, S, and D. We suggest that Hedin described CatG activity in bovine spleen over 100 years ago.
4

The effects of Fasciola hepatica infection on the total antioxidant status (TAS) and the activity of proteases and their inhibitors in rat serum

84%
Kolodziejczyk L., Jarocka I., Skrzydlewska E.
Folia Biologica
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2013
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tom 61
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nr 3-4
5

A tolerogenic role of cathepsin G in a primate model of multiple sclerosis: abrogation by Epstein–Barr virus infection

84%
Hart B. A.
Archivum Immunologiae et Therapiae Experimentalis
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2020
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tom 68
|
nr 4
6

Activity-based protein profiling of serine proteases in immune cells

84%
Kahler J. P., Vanhoutte R., Verhelst S. H. L.
Archivum Immunologiae et Therapiae Experimentalis
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2020
|
tom 68
|
nr 4
7

Isolation and amino-acid sequence of two inhibitors of serine proteinase, members of the squash inhibitor family, from Echinocystis lobata seeds

84%
Stachowiak D., Polanowski A., Bieniarz G., Wilusz T.
Acta Biochimica Polonica
|
1996
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tom 43
|
nr 3
Two serine proteinase inhibitors (ELTII and ELT1II) have been isolated from mature seeds of Echinocystis lobata by ammonium sulfate fractionation, methanol preci­pitation, ion exchange chromatography, affinity chromatography on immobilized anhydrotrypsin and HPLC. ELTI I and ELTI II consist of 33 and 29 amino-acid residues, respectively. The primary structures of these inhibitors are as follows: ELTI I KEEQRVCPRILMRCKRDSDCLAQCTCQQSGFCG ELTI II RVCPRILMRCKRDSDCLAQCTCQQSGFCG The inhibitors show sequence similarity with the squash inhibitor family. ELTI I differs from ELTI II only by the presence of the NH2-terminal tetrapeptide Lys- -Glu-Glu-Gln. The association constants (Ka) of F.LTI I and ELTI II with bovine-trypsin were determined to be 6.6 x 1010 M -1 and 3.1 x 1011 M -1, whereas the association constants of these inhibitors with cathepsin G were 1.2 x 107 M -1 and 1.1 x 107 M -1, respectively.
8

Cathepsin G and its dichotomous role in modulating levels of MHC class I molecules

67%
Burster T., Knippschild U., Molnar F., Zhanapiya A.
Archivum Immunologiae et Therapiae Experimentalis
|
2020
|
tom 68
|
nr 4
9

The effect of U83836E on the proteolytic-antiproteolytic balance in plasma of rats after methanol ingestion

67%
Skrzydlewska E., Roszkowska A., Farbiszewski R.
Acta Poloniae Toxicologica
|
1999
|
tom 07
|
nr 2
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