Purification and characterization of cystatin from duck egg white.

M Warwas; J Gburek; J Osada; K Gołab

doi:10.18388/abp.1995_4633

Purification and characterization of cystatin from duck egg white.

M Warwas Department of Pharmaceutical Biochemistry, Medical Academy, Wrocław, Poland.;
J Gburek
J Osada
K Gołab

DOI: https://doi.org/10.18388/abp.1995_4633

Abstract

It is the second peptidase inhibitor, after ovostatin, which showing the same antipapain activity in egg white in different avian species implies differences in amino-acid sequences. Cystatin from duck egg white was purified by carboxymethylpapain affinity chromatography and size-exclusion HPLC. The purified inhibitor which showed partial identity in the immunodiffusion test with chicken egg white cystatin, had an apparent molecular mass of 9.3 kDa as determined by SDS/PAGE. IEF analysis revealed five molecular forms of pI in the range 7.8-8.4. The obtained cystatin was neither glycosylated nor phosphorylated as it is in the case of chicken cystatin. The determined Ki (0.005 +/- 0.001 nM) was similar to that reported for human and chicken cystatin C.

Published

1995-09-30

Issue

Vol. 42 No. 3 (1995)

Section

Articles

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