TY - JOUR
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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U2 - 10.1111/j.1399-3011.1996.tb00829.x
DO - 10.1111/j.1399-3011.1996.tb00829.x
M3 - Article
C2 - 8872536
AN - SCOPUS:0029780852
VL - 48
SP - 174
EP - 181
JO - International journal of protein research
JF - International journal of protein research
SN - 0367-8377
IS - 2
ER -