Characterization of a trypsin inhibitor from equine urine.
A trypsin inhibitor was isolated from pregnant mares' urine by adsorption on bentonite and elution with aqueous pyridine followed by batch DEAE-cellulose treatment and column chromatography. Final purification to an electrophoretically homogenous glycoprotein was achieved by gel permeation chromatography. This equine urinary trypsin inhibitor (E-UTI) is acid- and heat-stable, has a molecular weight of 22 to 23 kDa, an isoelectric point of 4.55, forms a 1:1 molar complex with trypsin and has serine as its N-terminal amino acid. The N-terminal amino acid sequence of this protein is almost identical with that of EI-14, the inhibitor obtained from horse serum by tryptic treatment, except for two extra amino acid residues, Ser-Lys- on the N-terminal end of E-UTI. In its isoelectric point E-UTI differs from EI-14 and the inhibitor from human urine.
Veeraragavan
K
K
Biotechnology Research Institute, National Research Council of Canada, Montreal.
Singh
K
K
Wachter
E
E
Hochstrasser
K
K
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D006736:Horses; D006801:Humans; D008969:Molecular Sequence Data; D011247:Pregnancy; D014361:Trypsin Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000652:urine*
D000596:Amino Acids; D014361:Trypsin Inhibitors