Biochemical and Biophysical Research Communications 1979-09-12

Degradation of bradykinin by isolated neutral endopeptidases of brain and pituitary.

S Wilk, M Orlowski

Index: Biochem. Biophys. Res. Commun. 90 , 1, (1979)

Full Text: HTML

Abstract

The degradation of bradykinin by a highly purified preparation of rabbit brain prolyl endopeptidase and by an apparently homogeneous preparation of a bovine pituitary cation-sensitive neutral endopeptidase was studied. Peptide fragments were separated and isolated by high performance liquid chromatography and identified by amino acid analysis. Prolyl endopeptidase rapidly cleaves bradykinin at the Pro 7-Phe 8 bond. A slower cleavage also occurs at the Pro 3-Gly 4 bond. Cation-sensitive neutral endopeptidase splits bradykinin at the Phe 5-Ser 6 bond. These enzymes may participate in the regulation of brain concentrations of bradykinin.

Related Compounds

  • Z-Gly-Gly-Leu-pN...

Related Articles:

A new chromogenic substrate for subtilisin.

1974-12-01

[Anal. Biochem. 62 , 371-376, (1974)]

Evidence that pituitary cation-sensitive neutral endopeptidase is a multicatalytic protease complex.

1983-03-01

[J. Neurochem. 40 , 842-849, (1983)]

A synthetic endopeptidase substrate hydrolyzed by the bovine lens neutral proteinase preparation.

1984-05-01

[Exp. Eye Res. 38(5) , 477-83, (1984)]

Activity of Subtilisin Carlsberg in macromolecular crowding.

2007-03-01

[J. Photochem. Photobiol. B, Biol. 86(3) , 199-206, (2007)]

Technical note: quantification of multicatalytic proteinase complex (proteasome) activity by ion-exchange chromatography.

1993-12-01

[J. Anim. Sci. 71(12) , 3301-6, (1993)]

More Articles...