Purification of two low-molecular-mass serine proteinase inhibitors from chicken liver
| Autor: | Agnieszka Łopuska, Tadeusz Wilusz, Antoni Polanowski, Jolanta Polanowska |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Phenylglyoxal
Serine Proteinase Inhibitors Arginine Molecular Sequence Data Peptide Cathepsin G Biochemistry Analytical Chemistry chemistry.chemical_compound Peptide bond Animals Humans Amino Acid Sequence Peptide sequence chemistry.chemical_classification Chromatography Molecular mass Organic Chemistry General Medicine Chromatography Ion Exchange Molecular biology Molecular Weight chemistry Liver Chromatography Gel Cattle Electrophoresis Polyacrylamide Gel Chickens |
| Zdroj: | Journal of chromatography. A. 852(1) |
| ISSN: | 0021-9673 |
| Popis: | Two serine proteinase inhibitors, designated clTI-1 and clTI-2 were purified from livers of chickens to apparent homogeneity by a combination of ethanol-acetone fractionation, gel filtration and ion-exchange chromatography on CM-cellulose and Mono S columns. The inhibitor clTI-1 is a single polypeptide chain, low-molecular-mass protein (Mr about 6200), very stable to heat and ethanol. It inhibits chicken, porcine and bovine trypsins as well as human plasmin. The second protein, lcTI-2 of Mr 17 000 was shown to be a very effective inhibitor of both trypsins and human cathepsin G. Since both inhibitors are sensitive to arginine modification with phenylglyoxal it is assumed that this amino acid residue is present at the P1 position of the reactive site peptide bond. The N-terminal amino acid sequence of 28 residues of clTI-2 (SVDVSKYPSTVSKDGRTLVACPRILSPV) revealed a high homology of this protein to the third domain of the chicken ovoinhibitor, whereas, the clTI-1 (APPAAEKYYSLPPGAPRYYSPVV) has some sequence identity to a fragment of the human inter-α-trypsin inhibitor. |
| Databáze: | OpenAIRE |
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