Formation of angiotensin II by tonin from partially purified human angiotensinogen.

@article{Gris1981FormationOA,
  title={Formation of angiotensin II by tonin from partially purified human angiotensinogen.},
  author={C Gris{\'e} and Roger Boucher and Ga{\'e}tan Thibault and Jacques J Genest},
  journal={Canadian journal of biochemistry},
  year={1981},
  volume={59 4},
  pages={250-5}
}
The renin substrate (angiotensinogen) has been purified from outdated human blood bank plasma. A 100-fold purification was achieved by ammonium sulphate protein fractionation and four successive chromatographic procedures. We show that tonin, a serine protease enzyme found in submaxillary glands of the rat, cleaves the human plasma angiotensinogen, devoid of tonin inhibiting factor(s), at a pH optimum of 5--5.5. It generates a pressor substance that was identified as angiotensin (A) II. The… CONTINUE READING

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