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The use of gel-filtration for the isolation of pure nisin from commercial products

100%

Wilimowska-Pelc A., Olichwier Z., Malicka-Blaszkiewicz M., Mejbaum-Katzenellenbogen W.

Acta Microbiologica Polonica

1976

tom 25

nr 1

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

88%

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

Acta Biochimica Polonica

1996

tom 43

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.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Acta Microbiologica Polonica

2 Olichwier Z.

2 Wilimowska-Pelc A.

1 Gladysz M.

1 Malicka-Blaszkiewicz M.

1 Mejbaum-Katzenellenbogen W.

1 Polanowski A.

1 Stachowiak D.

1 1996

1 1976

Wyniki wyszukiwania

The use of gel-filtration for the isolation of pure nisin from commercial products

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