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1

Disulfide bonds in protein folding studies: friends or foes?

100%

Dadlez M.

Acta Biochimica Polonica

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1997

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tom 44

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nr 3

The studies on protein folding pathways utilizing disulfide bonds as reporter groups in several protein model systems arc reviewed. Implications for a general mechanism of protein folding are discussed. An updated folding pathway for bovine pancreatic trypsin inhibitor (BPTI) based on recent data is proposed.

2

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Effect of Ascaris trypsin inhibitor on fetal development of mice

88%

Blaszkowska J.

Wiadomości Parazytologiczne

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2005

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tom 51

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nr 2

In this study, maternal toxicity and developmental effects of exposure to Ascaris trypsin inhibitor were evaluated in mice. Pregnant BALB/c females were injected intraperitoneally by Ascaris inhibitor /AIT/ at 200, 300, and 400 mg/kg body weight/day, on days 12 to 15 of gestation (stage of fetal development). At day 19 of pregnancy, uterine contents were inspected for implantation sites, early resorptions (moles), living fetuses and dead fetuses. The living fetuses were weighed and examined for external, internal and skeletal abnormalities. The results showed that AIT induced maternal toxicity, evidenced by maternal deaths, abortions, bleeding from uterus and reduced body weight gain as compared to control (p <0.01). There were no differences between the control group and the rest of all groups investigated for total implantation sites and early resorptions. Fetotoxicity was observed as shown by the decrease in the number of living fetuses and mean fetal weight, a high rate of intrauterine fetal deaths, delayed skeletal ossification, occurrence of pathological changes of fetal organs and tissues. Only one type of congenital malformations (hydronephrosis) was noted in fetuses after injection of higher doses of AIT.

3

Purification and characterization of trypsin inhibitor from seeds of faba bean [Vicia faba L.]

88%

Gupta P., Dhawan K., Malhotra S. P., Singh R.

Acta Physiologiae Plantarum

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2000

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tom 22

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nr 4

4

Effects of far infrared treatment on lipoxygenase activity and antinutritional factors of soybean samples

75%

Basman A., Yalcin S.

Polish Journal of Food and Nutrition Sciences

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2011

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tom 61

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nr Suppl.1

5

The effect of Ascaris lumbricoides suis trypsin inhibitor on hydrolytic activity of developing ascarid eggs

75%

Wojcik A., Blaszkowska J.

Wiadomości Parazytologiczne

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1998

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tom 44

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nr 3

6

Comparison of the effect of Ascaris trypsin inhibitor and ovomucoid on fetal development in mice

75%

Blaszkowska J., Wojcik A.

Wiadomości Parazytologiczne

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1998

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tom 44

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nr 3

7

Trypsin inhibitor electrophoretic patterns in Vicia faba L. and related species

75%

Zimniak-Przybylska Z., Przybylska J., Krajewski P.

Journal of Applied Genetics

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1999

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tom 40

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nr 4

8

Aspartic proteinase from the seeds of figleaf gourd [Cucurbita ficifolia]

75%

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

Acta Biochimica Polonica

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1994

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tom 41

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nr 2

9

Factors improving the accuracy of determination of 15N relaxation parameters in proteins

75%

Zhukov I., Ejchart A.

Acta Biochimica Polonica

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1999

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tom 46

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nr 3

A number of factors at all stages of data processing which affect the accuracy of determination of 15N relaxation parameters in 15N-labeled proteins is discussed. Methods which allow to improve accuracy of the determined parameters are presented using data obtained for Cucurbita maxima trypsin inhibitor.

10

The effect of Ascaris lumbricoides suis trypsin inhibitor on RNA, DNA and protein biosyntheses in developing A.lumbricoides suis eggs - Part II

63%

Ochecka-Szymanska A., Turski W. A.

Wiadomości Parazytologiczne

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1998

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tom 44

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nr 3

11

Comparison of the effect of Ascaris trypsin inhibitor in various periods of mouse pregnancy

63%

Blaszkowska J.

Wiadomości Parazytologiczne

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2001

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tom 47

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nr 4

Trypsin inhibitor isolated from Ascaris suum and injected into pregnant BALB/c mice (five times, in doses: 300 or 400 mg/kg/day) in various periods of pregnancy (early and late organogenesis) disturbed the development of fetuses. The nature and intensity of prenatal disturbances are determined by the inhibitor dose and time of injection. It has been found that administration of the inhibitor from 5-th until 9-th day of gestation did not delay or prevent implantation, but caused a high rate of- intrauterine deaths and also specific congenital malformations (exnencephaly and hydrocephalus). Additionally, other types of defects were noted in fetuses after injection of the inhibitor between 8-th and 12-th day of pregnancy (cleft palate, fusion of ribs). Independent of the time of injection during gestation the inhibitor exhibited embriotoxic effects (e.g. decreased the number of live fetuses per litter and mean fetal weight).

12

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

63%

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

Acta Biochimica Polonica

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1996

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tom 43

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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.

13

Disturbances of mouse pregnancy after injection of Ascaris trypsin inhibitor during early organogenesis

63%

Blaszkowska J.

Zoologica Poloniae

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1999

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tom 44

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nr 1-4

14

The effect of proteolysis inhibitors from Ascaris lumbricoides suis on developing chicken embryos

63%

Blaszkowska J., Wojcik A.

Wiadomości Parazytologiczne

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1998

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tom 44

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nr 3

15

The effect of Ascaris lumbricoides suis trypsin inhibitor on RNA, DNA, and protein biosyntheses in developing A.lumbricoides suis eggs - Part I

63%

Ochecka-Szymanska A., Turski W. A.

Wiadomości Parazytologiczne

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1998

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tom 44

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nr 3

16

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

63%

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

Acta Biochimica Polonica

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1995

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tom 42

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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.

17

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

63%

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

Acta Societatis Botanicorum Poloniae

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2003

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tom 72

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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.

18

Structure-function relationship of serine protease-protein inhibitor interaction

63%

Otlewski J., Jaskolski M., Buczek O., Cierpicki T., Czapinska H., Krowarsch D., Smalas A. O., Stachowiak D., Szpineta A., Dadlez M.

Acta Biochimica Polonica

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2001

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tom 48

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nr 2

We re port our prog ress in un der stand ing the struc ture-function re la tion ship of the interaction between protein inhibitors and several serine proteases. Recently, we have de ter mined high res o lu tion so lu tion struc tures of two in hib i tors Apis mellifera chymotrypsin in hib i tor-1 (AMCI-I) and Linum usitatissimumtrypsin in hib i tor (LUTI) in the free state and an ul tra high res o lu tion X-ray struc ture of BPTI. All three in hib i tors, de spite to tally dif fer ent scaf folds, con tain a sol vent ex posed loop of sim i lar con- for ma tion which is highly com ple men tary to the en zyme ac tive site. Iso ther mal calorim e try data show that the in ter ac tion be tween wild type BPTI and chymotrypsin is entropy driven and that the enthalpy com po nent op poses com plex for ma tion. Our research is fo cused on ex ten sive mu ta gen e sis of the four po si tions from the pro te ase bind ing loop of BPTI: P1, P1', P3, and P4. We mu tated these res i dues to dif fer ent amino ac ids and the vari ants were char ac ter ized by de ter mi na tion of the as so ci a tion con stants, sta bil ity pa ram e ters and crys tal struc tures of pro te ase–in hib i tor complexes. Ac com mo da tion of the P1 res i due in the S1 pocket of four pro teas es: chymotrypsin, trypsin, neutrophil elastase and cathepsin G was probed with 18 P1 vari ants. High res o lu tion X-ray struc tures of ten com plexes be tween bo vine trypsin and P1 vari ants of BPTI have been de ter mined and com pared with the cog nate P1 Lysside chain. Mu ta tions of the wild type Ala16 (P1') to larger side chains al ways caused a drop of the as so ci a tion con stant. Ac cord ing to the crys tal struc ture of the Leu16 BPTI–trypsin com plex, in tro duc tion of the larger res i due at the P1' po si tion leads to steric con flicts in the vi cin ity of the mu ta tion. Finally, mu ta tions at the P4 site al lowed an im prove ment of the as so ci a tion with sev eral serine pro teas es in volved in blood clot ting. Con versely, in tro duc tion of Ser, Val, and Phe in place of Gly12 (P4) had invariably a destabilizing ef fect on the com plex with these pro teas es.

19

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

63%

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

Acta Biochimica Polonica

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1996

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tom 43

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nr 3

A trypsin inhibitor of Kazal type has been isolated from goose pancreas by affinity chromatography on immobilized anhydrotrypsin, anion exchange and reverse phase HPLC. It inhibits bovine β-trypsin with the association constant (Ka) of 5.99 x 10 M-1. The complete amino-acid sequence was determined following CNBr treatment. The protein comprised a total of 69 amino-acid residues, corresponding to a molecular mass of 7.7 kDa. The P1-P'1 reactive site bond of the inhibitor was localized at position Lys25-Met26. The amino-acid sequence of GPTI shows extremely high homology to that of other inhibitors isolated from pancreas of birds.

20

The influence of extrusion or boiling on trypsin inhibitor and lectin activity in leguminous seeds and protein digestibility in rats

63%

Leontowicz H., Leontowicz M., Kostyra H., Gralak M. A., Kulasek G. W.

Polish Journal of Food and Nutrition Sciences

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1999

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tom 08

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nr 4

Raw seeds (R) of pea (P), faba bean (F), and soybean (S) were extruded at 130, 150 or 170°C, or boiled in water without previous soaking for 5, 10 or 20 min. Trypsin inhibitors activity (TIA) in raw seeds of P, F and S amounted 2.3, 2.1 and 31.3, and after extrusion at 170°C it reached 0.1, 0.5 and 8.5 trypsin unit inhibited/mg sample (TIU/mg) in P, F and S, respectively. Ten minutes exposition in boiled water decreased TIA to 0.1, 0.1 and 0.4 TIU/mg, respectively. Haemagglutinin activity (HAA) assayed in raw seeds with guinea pig erythrocytes was 400, 100 and 800 in Ę F and S, respectively. Extrusion at 170°C decreased HAA to 100, 0 and 100 in P, F and S, respectively. Extracts from faba bean and pea which had been boiled for 20 min did not agglutinate human erythrocytes. However, boiled soybean still showed agglutination activity at 200, 200, 100 and 400 for blood groups: 0, A, В and AB, respectively It is concluded that for the nutritional purpose extrusion at 150°C is adequate for elimination of TIA and HAA in P and F, but in the case of S 170°C is required. However, ten minutes of exposition of raw seeds to boiling water is effective for elimination of TIA. Boiling for twenty minutes canceled HAA in faba bean and pea protein extracts, but it was not so efficient in the case of soybean. Rats fed diets with 10% of extruded leguminous seeds (150°C) had significantly increased apparent digestibility of dry matter and crude protein.

Ograniczanie wyników

Disulfide bonds in protein folding studies: friends or foes?

Effect of Ascaris trypsin inhibitor on fetal development of mice

Purification and characterization of trypsin inhibitor from seeds of faba bean [Vicia faba L.]

Effects of far infrared treatment on lipoxygenase activity and antinutritional factors of soybean samples

The effect of Ascaris lumbricoides suis trypsin inhibitor on hydrolytic activity of developing ascarid eggs

Comparison of the effect of Ascaris trypsin inhibitor and ovomucoid on fetal development in mice

Trypsin inhibitor electrophoretic patterns in Vicia faba L. and related species

Aspartic proteinase from the seeds of figleaf gourd [Cucurbita ficifolia]

Factors improving the accuracy of determination of 15N relaxation parameters in proteins

The effect of Ascaris lumbricoides suis trypsin inhibitor on RNA, DNA and protein biosyntheses in developing A.lumbricoides suis eggs - Part II

Comparison of the effect of Ascaris trypsin inhibitor in various periods of mouse pregnancy

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

Disturbances of mouse pregnancy after injection of Ascaris trypsin inhibitor during early organogenesis

The effect of proteolysis inhibitors from Ascaris lumbricoides suis on developing chicken embryos