Search results

1

Isolation and partial characterization of the trypsin inhibitor from the seeds of Brassica oleracea var. sabellica

100%

Wilimowska-Pelc A.

|

vol. 32

|

issue 4

351-361

2

Aspartyl proteinase from cucumber (Cucumis sativus) seeds. Preparation and characteristics

72%

Wilimowska-Pelc A., Polanowski A., Kołaczkowska M. K., Wieczorek M., Wilusz T.

Acta Biochimica Polonica

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1983

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vol. 30

|

issue 1

23-31

3

Antiproteolytic activity of goose pancreas: Purification, inhibitory properties and amino-acid sequence of a Kazal type trypsin inhibitor

72%

Wilimowska-Pelc A., Stachowiak D., Gładysz M., Olichwier Z., Polanowski A.

Acta Biochimica Polonica

|

1996

|

vol. 43

|

issue 3

489-496

4

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

62%

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

|

2003

|

vol. 50

|

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.

5

Protein inhibitors of trypsin from the seeds of Cucurbitaceae plants

62%

Polanowski A., Cieślar E., Otlewski J., Nienartowicz B., Wilimowska-Pelc A., Wilusz T.

|

issue 4

395-406

6

Aspartic proteinase from the seeds of figleaf gourd (Cucurbita ficifolia)

62%

Stachowiak D., Wilimowska-Pelc A., Kołaczkowska M., Polanowski A., Wilusz T., Larsen L. B.

Acta Biochimica Polonica

|

1994

|

vol. 41

|

issue 2

181-182

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1 Kowalska J.

1 Kołaczkowska M.

1 Kołaczkowska M. K.

1 Larsen L. B.

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1 Otlewski J.

1 Wieczorek M.

1 Żelazko M.

Isolation and partial characterization of the trypsin inhibitor from the seeds of Brassica oleracea var. sabellica

Aspartyl proteinase from cucumber (Cucumis sativus) seeds. Preparation and characteristics

Antiproteolytic activity of goose pancreas: Purification, inhibitory properties and amino-acid sequence of a Kazal type trypsin inhibitor

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

Protein inhibitors of trypsin from the seeds of Cucurbitaceae plants

Aspartic proteinase from the seeds of figleaf gourd (Cucurbita ficifolia)