Purification and characterization of a trypsin inhibitor from mouse seminal vesicle secretion.

@article{Lai1991PurificationAC,
  title={Purification and characterization of a trypsin inhibitor from mouse seminal vesicle secretion.},
  author={M L Lai and S W Chen and Yi Hsuan Chen},
  journal={Archives of biochemistry and biophysics},
  year={1991},
  volume={290 2},
  pages={265-71}
}
A Kazal-type trypsin inhibitor in mouse seminal vesicle secretion was purified to homogeneity via a series of purification steps including ammonium sulfate fractionation, affinity chromatography on a trypsin Affi-Gel 10 column, and HPLC on a reverse phase C4 column. It was shown to be a weak basic protein with an isoelectric point of 8.7 and to contain no carbohydrate. The protein had a specific activity of 184 U/mg protein in the inhibitory effect on the trypsin digestion of N-benzoyl-Pro-Phe… CONTINUE READING
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