Wyniki wyszukiwania

1

The serine proteinase inhibitor from summer squash (Cucurbita pepo): sme structural features, stability and proteolytic degradation

100%

Otlewski J., Wilusz T.

Acta Biochimica Polonica

|

1985

|

tom 32

|

nr 4

2

Aktywność biologiczna białek ekstrahujących się kwasem sulfosalicylowym z tarczyc ludzkich i zwierzęcych

100%

Wieczorek E., Wilusz T.

Acta Physiologica Polonica

|

1970

|

tom 21

|

nr 2

3

Serine proteinase inhibitors from insect hemolymph

100%

Polanowski A., Wilusz T.

Acta Biochimica Polonica

|

1996

|

tom 43

|

nr 3

Insect hemolymph, like vertebrate serum, contains several different types of polypeptides that are able to inhibit the catalytic function of proteolytic enzymes, however studies on proteins possessing this capability have been limited to a relatively few species. A comparative examination of the inhibition of trypsin, chymo- trypsin, neutrophil elastase and cathepsin G and pancreatic elastase by the hemolymph of 14 insect species belonging to six orders showed great diversity in terms of both total proteinase inhibitory capacity and specificity. Most of the inhibitors examined fall into two groups: low molecular mass proteins (below 10 kDa) related to Kunitz type inhibitors, and proteins of about 45 kDa which belong to the serpin superfamily of serine proteinase inhibitors. This minireview describes the properties, characteristics and possible biological significance of selected inhibitors.

4

The use immobilized methylchymotrypsin for the purification of human and sheep alpha-1-proteinase inhibitor [alpha1-PI]

100%

Grybel J., Wilusz T.

Cellular and Molecular Biology Letters

|

2003

|

tom 08

|

nr 2

α1-proteinase inhibitor was isolated from albumin fractions of human and sheep plasma using a new method of purification using affinity chromatography on immobilized methylchymotrypsin in the presence of 5 M NaCl. The inhibitor was finally polished to homogenity either by chromatography on a Mono Q or a Sephacryl S-200 HR column. The presented method makes it possible to recover α1-proteinase inhibitor which has been added to cow milk.

5

Determination and preparation of the products of enzymic degradation of protein

81%

Mejbaum-Katzenellenbogen W., Wilusz T., Polanowski A.

Acta Biochimica Polonica

|

1966

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tom 13

|

nr 1

6

Trypsin inhibitors in bovine lung and pancreas during development

81%

Wilusz T., Wilimowska-Pelec A., Mejbaum-Katzenellenbogen W.

Acta Biochimica Polonica

|

1976

|

tom 23

|

nr 2-3

7

Isolation of two trypsin inhibitors from resting seeds of the white bush (Cucurbita pepo var. patissonina) and their properties

81%

Pham T. C., Leluk J., Wilusz T., Polanowski A.

Acta Biochimica Polonica

|

1985

|

tom 32

|

nr 4

8

Trypsin inhibitors in summer squash ( Cucurbita pepo) seeds. Isolation, purification and partial characterization of three inhibitors

81%

Otlewski J., Polanowski A., Leluk J., Wilusz T.

Acta Biochimica Polonica

|

1984

|

tom 31

|

nr 3

9

An improved method of isolation of crystalline basic trypsin inhibitor from bovine tissues

81%

Wilusz T., Lomako J., Mejbaum-Katzenellenbogen W.

Acta Biochimica Polonica

|

1973

|

tom 20

|

nr 1

10

Thioredoxin and thioredoxin-like proteins accompanying a trypsin inhibitor purification from garlic bulbs (Allium sativum)

81%

Lorenc-Kubis I., Zuziak E., Grad B., Wilusz T.

Acta Biochimica Polonica

|

2003

|

tom 50

|

nr Supplement 1

11

Participation of polypeptide proteinase inhibitors in proliferation of fibroblasts

81%

Popik W., Inglot A. D., Wilusz T., Polanowski A.

Archivum Immunologiae et Therapiae Experimentalis

|

1988

|

tom 36

|

nr 5

12

1 H NMR spectra of trypsin inhibitors from seeds of Cucurbitaceae plants, resonance signals of methyl groups

81%

Siemion I., Sobczak K., Wilusz T., Polanowski A.

Acta Biochimica Polonica

|

1984

|

tom 31

|

nr 2

13

Amino acid sequence of the basic trypsin inhibitor from bovine splenic capsule. A new fluorescent reagent for protein sequence analysis

81%

Nowak K., Kuczek M., Slominska A., Wilusz T.

Acta Biochimica Polonica

|

1977

|

tom 24

|

nr 4

14

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

81%

Stachowiak D., Polanowski A., Bieniarz G., Wilusz T.

Acta Biochimica Polonica

|

1996

|

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.

15

Synthesis, cloning and expression in Escherichia coli of the gene coding for the trypsin inhibitor from Cucurbita pepo

81%

Rempola B., Wilusz T., Markiewicz W., Fikus M.

Acta Biochimica Polonica

|

1995

|

tom 42

|

nr 1

A chemically synthesized gene coding for the serine proteinase inhibitor CPTI II was cloned in E. coli and its expression was investigated in cytoplasmic and secretion systems. Under all conditions investigated the biologically active form of the inhibitor was found only in the latter system, although the yield was rather low.

16

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Does the oxidation of methionine residue precede the inactivation of the trypsin inhibitor [LUTI] in germinating seeds of common flax [Linum usitatissimum]?

81%

Lorenc-Kubis I., Czerwinska-Golen A., Kowalska J., Wilusz T.

Acta Societatis Botanicorum Poloniae

|

2003

|

tom 72

|

nr 4

Antitrypsin activity in germinating common seeds of flax (Linum usitatissimum) was investigated. At the early stage of germination an increase in antitrypsin activity was observed, followed by its decrease during the development of the seedlings. From 6-day-old seedlings a trypsin inhibitor (gerLUTI) was purified. The purification procedure involved fractionation of proteins from seedling homogenate with alcohol and successive chromatography on CM-Sephadex C-25 on immobilised methylchymotrypsin in the presence of 5 M NaCl, and finally on a C18 column in RP-HPLC. The gerLUTI migrated in SDS PAGE as a single band, but in mass spectroscopy analysis it exhibited the presence of at least three forms with molecular masses of 7654 ± 3 Da, 7668/7670 ± 3 Da, and 7687 ± 3 Da. The preparation of LUTI isolated from resting seeds contained only one form, with a molecular mass of 7655 ± 3 Da. LUTI and gerLUTI differed also in methionine contents. LUTI contained two methionine residues, whereas in gerLUTI only a trace of methionine was detected. The obtained results might suggest that during flax seeds germination the inhibitor molecules undergo selective modification, e.g. oxidation at methionine residues, before being degraded by proteolytic enzymes.

17

Two serine proteinase inhibitors from the larval hemolymph of Heliothis zea

81%

Polanowski A., Wilusz T., Blum M. S., Travis J.

Acta Biochimica Polonica

|

1994

|

tom 41

|

nr 2

18

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

81%

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).

19

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

71%

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

Acta Biochimica Polonica

|

1983

|

tom 30

|

nr 1

20

Preparation and characteristics of trypsin inhibitors from the seeds of squash (Cucurbita maxima) and zucchini (Cucurbita pepo, vcir. Giromontia)

71%

Leluk J., Otlewski J., Wieczorek M., Polanowski A., Wilusz T.

Acta Biochimica Polonica

|

1983

|

tom 30

|

nr 2

Ograniczanie wyników

The serine proteinase inhibitor from summer squash (Cucurbita pepo): sme structural features, stability and proteolytic degradation

Aktywność biologiczna białek ekstrahujących się kwasem sulfosalicylowym z tarczyc ludzkich i zwierzęcych

Serine proteinase inhibitors from insect hemolymph

The use immobilized methylchymotrypsin for the purification of human and sheep alpha-1-proteinase inhibitor [alpha1-PI]

Determination and preparation of the products of enzymic degradation of protein

Trypsin inhibitors in bovine lung and pancreas during development

Isolation of two trypsin inhibitors from resting seeds of the white bush (Cucurbita pepo var. patissonina) and their properties

Trypsin inhibitors in summer squash ( Cucurbita pepo) seeds. Isolation, purification and partial characterization of three inhibitors

An improved method of isolation of crystalline basic trypsin inhibitor from bovine tissues

Thioredoxin and thioredoxin-like proteins accompanying a trypsin inhibitor purification from garlic bulbs (Allium sativum)

Participation of polypeptide proteinase inhibitors in proliferation of fibroblasts

1 H NMR spectra of trypsin inhibitors from seeds of Cucurbitaceae plants, resonance signals of methyl groups

Amino acid sequence of the basic trypsin inhibitor from bovine splenic capsule. A new fluorescent reagent for protein sequence analysis

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

Synthesis, cloning and expression in Escherichia coli of the gene coding for the trypsin inhibitor from Cucurbita pepo

Does the oxidation of methionine residue precede the inactivation of the trypsin inhibitor [LUTI] in germinating seeds of common flax [Linum usitatissimum]?

Two serine proteinase inhibitors from the larval hemolymph of Heliothis zea

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

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

Preparation and characteristics of trypsin inhibitors from the seeds of squash (Cucurbita maxima) and zucchini (Cucurbita pepo, vcir. Giromontia)