Purification and characterization of ostrich pancreatic secretory trypsin inhibitor

Ming Zhao; Ryno J. Naudé; Koji Muramoto

doi:10.1111/j.1399-3011.1996.tb00829.x

Purification and characterization of ostrich pancreatic secretory trypsin inhibitor

Ming Zhao, Ryno J. Naudé, Koji Muramoto

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Abstract

Ostrich pancreatic secretory trypsin inhibitor was isolated and purified using acid extraction, salt fractionation, SP-Sephadex C-50 and QAE-Sephadex A-25 chromatography and RP-HPLC. The amino acid sequence of ostrich PSTI showed it is a single peptide chain containing 69 amino acid residues with the highest homology between ostrich and chicken PSTI. The molecular weight, as determined by electronspray mass spectrometry and from amino acid sequence data, is 7650 Da. The isoelectric point of ostrich PSTI was found to be 5.7. Ostrich PSTI specifically inhibited ostrich and commercial bovine trypsin with K(i) values of 8.0 x 10^-9 and 2.4 x 10^-7 M, respectively, while no inhibitory effects were observed with other serine proteases.

Original language	English
Pages (from-to)	174-181
Number of pages	8
Journal	International Journal of Peptide and Protein Research
Volume	48
Issue number	2
DOIs	https://doi.org/10.1111/j.1399-3011.1996.tb00829.x
Publication status	Published - 1996

Keywords

Amino acid sequence
Kazal inhibitor
Ostrich
Pancreatitic secretory trypsin inhibitor

ASJC Scopus subject areas

Biochemistry

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abstract = "Ostrich pancreatic secretory trypsin inhibitor was isolated and purified using acid extraction, salt fractionation, SP-Sephadex C-50 and QAE-Sephadex A-25 chromatography and RP-HPLC. The amino acid sequence of ostrich PSTI showed it is a single peptide chain containing 69 amino acid residues with the highest homology between ostrich and chicken PSTI. The molecular weight, as determined by electronspray mass spectrometry and from amino acid sequence data, is 7650 Da. The isoelectric point of ostrich PSTI was found to be 5.7. Ostrich PSTI specifically inhibited ostrich and commercial bovine trypsin with K(i) values of 8.0 x 10-9 and 2.4 x 10-7 M, respectively, while no inhibitory effects were observed with other serine proteases.",

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author = "Ming Zhao and Naud{\'e}, {Ryno J.} and Koji Muramoto",

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T1 - Purification and characterization of ostrich pancreatic secretory trypsin inhibitor

AU - Zhao, Ming

AU - Naudé, Ryno J.

AU - Muramoto, Koji

PY - 1996

Y1 - 1996

N2 - Ostrich pancreatic secretory trypsin inhibitor was isolated and purified using acid extraction, salt fractionation, SP-Sephadex C-50 and QAE-Sephadex A-25 chromatography and RP-HPLC. The amino acid sequence of ostrich PSTI showed it is a single peptide chain containing 69 amino acid residues with the highest homology between ostrich and chicken PSTI. The molecular weight, as determined by electronspray mass spectrometry and from amino acid sequence data, is 7650 Da. The isoelectric point of ostrich PSTI was found to be 5.7. Ostrich PSTI specifically inhibited ostrich and commercial bovine trypsin with K(i) values of 8.0 x 10-9 and 2.4 x 10-7 M, respectively, while no inhibitory effects were observed with other serine proteases.

AB - Ostrich pancreatic secretory trypsin inhibitor was isolated and purified using acid extraction, salt fractionation, SP-Sephadex C-50 and QAE-Sephadex A-25 chromatography and RP-HPLC. The amino acid sequence of ostrich PSTI showed it is a single peptide chain containing 69 amino acid residues with the highest homology between ostrich and chicken PSTI. The molecular weight, as determined by electronspray mass spectrometry and from amino acid sequence data, is 7650 Da. The isoelectric point of ostrich PSTI was found to be 5.7. Ostrich PSTI specifically inhibited ostrich and commercial bovine trypsin with K(i) values of 8.0 x 10-9 and 2.4 x 10-7 M, respectively, while no inhibitory effects were observed with other serine proteases.

KW - Amino acid sequence

KW - Kazal inhibitor

KW - Ostrich

KW - Pancreatitic secretory trypsin inhibitor

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Purification and characterization of ostrich pancreatic secretory trypsin inhibitor

Abstract

Keywords

ASJC Scopus subject areas

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