Wyniki wyszukiwania

1

Proteolytic activity of Pseudomonas chlororaphis 5N isolated from rhizosphere soil

100%

Jankiewicz U., Frak M.

Electronic Journal of Polish Agricultural Universities. Series: Biotechnology

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2012

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tom 15

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nr 4

2

The molecular and biochemical characteristics of proline iminopeptidase from rye seedlings [Secale cereale L.]

100%

Szawlowska U., Prus W., Bielawski W.

Acta Physiologiae Plantarum

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2006

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tom 28

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nr 6

A proline iminopeptidase (EC. 3.4.11.5) was isolated from shoots of 3 day old seedlings. The purification procedure consisted of 5 steps: acid precipitation, gel filtration on Sephadex G-200, ion-exchange chromatography on Sepharose CL 6B, twice repeated hydrophobic chromatography on Phenyl-Sepharose HP. The enzyme was purified 404.8-fold, with the specific activity of 8.5 units·mg⁻¹ of protein with recovery yield of 3 %. The purified enzyme had a molecular mass of 225 kDa estimated by gel filtration and 55.4 kDa by SDS PAGE. This indicates that native enzyme is composed of four subunits. The enzyme was specific for proline β-naphtylamide among various amino acid β-naphtylamides. An optimal activity was observed at 37 °C at pH 7.75. The enzyme was thermostable up to 37 °C for 30 min. The enzyme was strongly inhibited by pHMB, E-64, heavy metal ions and partially by PMSF, DFP. The results suggest that cysteine and serine residues may participate in the enzyme activity.

3

The properties and functions of bacterial aminopeptidases

80%

Jankiewicz U., Bielawski W.

Acta Microbiologica Polonica

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2003

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tom 52

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nr 3

4

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The directed enzymatic casein hydrolysis

80%

Idziak J., Moszczynski P.

Polish Journal of Food and Nutrition Sciences

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1993

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tom 02

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nr 1

5

Acid aspartate proteinase activity in fungal strains isolated from the oral cavity of patients with neoplasms

80%

Rozga A., Kurnatowska A. J., Loga G., Raczynska-Witonska G.

Wiadomości Parazytologiczne

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1998

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tom 44

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nr 3

6

Muscle cathepsins of marine fish and invertebrates

61%

Kolodziejska I., Sikorski Z. E.

Polish Journal of Food and Nutrition Sciences

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1995

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tom 04

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nr 3

Muscle proteases are located mainly in the lysosomes, in the sarcoplasm, and in the extracellular matrix of the connective tissue surrounding each cell. The lysosomal proteases, cathepsins, have optimum activity in the acidic range, although many of them retain high activity also 1 or 2 pH units away from the optimum value. Among the cathepsins there are endopeptidases and exopeptidases. Most cathepsins hydrolyse several proteins of the myofibrils. The major protease of the lysosomes in fish and squid muscles is cathepsin D, an aspartyl endoproteinase. Although it is present in the muscle fibre itself, its generally rather low activity at low temperature limits its significance in tenderization of refrigerated fish of most species. Cathepsin L, a cysteinyl protease, is involved in autolysis and softening in matured chum salmon. Cathepsin B, a cysteinyl carboxypeptidase, is capable to attack also some myofibrillar proteins. Cathepsin A or carboxypeptidase A, and cathepsin C, a dipeptidyl hydrolase and dipeptidyl transferase, contribute to the hydrolysis of muscle proteins in a concerted action with the other cathepsins.

Ograniczanie wyników

2 Polish Journal of Food and Nutrition Sciences

1 Acta Microbiologica Polonica

1 Acta Physiologiae Plantarum

1 Electronic Journal of Polish Agricultural Universities. Series: Biotechnology

1 Wiadomości Parazytologiczne

2 Bielawski W.

2 Jankiewicz U.

1 Frak M.

1 Idziak J.

1 Kolodziejska I.

1 Kurnatowska A. J.

1 Loga G.

1 Moszczynski P.

1 Prus W.

1 Raczynska-Witonska G.

1 Rozga A.

1 Sikorski Z. E.

1 Szawlowska U.

1 2012

1 2006

1 2003

1 1998

1 1995

1 1993

Proteolytic activity of Pseudomonas chlororaphis 5N isolated from rhizosphere soil

The molecular and biochemical characteristics of proline iminopeptidase from rye seedlings [Secale cereale L.]

The properties and functions of bacterial aminopeptidases

The directed enzymatic casein hydrolysis

Acid aspartate proteinase activity in fungal strains isolated from the oral cavity of patients with neoplasms

Muscle cathepsins of marine fish and invertebrates