PMID: 6161209Jan 1, 1980Paper

Screening for rabbit brain neuropeptide-metabolizing peptidases. Inhibition of endopeptidase B by bradykinin potentiating peptide 9a (SQ 20881)

Journal of Neurochemistry
A R MartinsA C Martins de Camargo

Abstract

Neutral thiol-activated peptidases present in the pH 5-soluble fraction of rabbit brain (separated by step-elution chromatography on diethylaminoethyl cellulose) were screened for the hydrolysis of bradykinin. Lys-bradykinin, Met-Lys-bradykinin, angiotensin I, angiotensin II, substance P, luteinizing hormone-releasing hormone (LH-RH), and neurotensin by bioassay. The column effluent was monitored for bradykinin inactivation and arylamidase activity and combined in six pools on the basis of bradykinin inactivation. The pools were characterized by determining the peptide fragments and amino acids released from bradykinin with an amino acid analyzer. Pools 1 through 3 contained 80% of the kininase activity and essentially all of the endopeptidase A and B activity, whereas pools 4 through 6 accounted for 98% of the recovered arylamidase activity. Bradykinin, angiotensin I, angiotensin II, and substance P were inactivated by all the pools, whereas LH-RH and neurotensin were inactivated by pools 3 and 4, and pools 3, 4, and 5, respectively. These data show that rabbit brain contains peptidases having some selectivity for the inactivation of neuropeptides. Endopeptidase B purified from pool 3 is inhibited by bradykinin-potentiating pe...Continue Reading

References

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Citations

Sep 1, 1989·Cellular and Molecular Neurobiology·E A DelBelA R Martins
Mar 1, 1985·Biulleten' eksperimental'noĭ biologii i meditsiny·L P Alekseenko, V N Orekhovich
Sep 11, 1987·Neuroscience Letters·A R MartinsF G De Mello
Feb 5, 1990·Neuroscience Letters·M L Nunes-MamedeA R Martins
Dec 1, 1985·Neurochemical Research·A M ArzumanyanT N Akopyan
Jun 1, 1981·Journal of Neurochemistry·K KariyaH Okamoto
Aug 1, 1987·Journal of Neurochemistry·F CheclerJ P Vincent
Sep 1, 1986·Journal of Neurochemistry·E A Del BelA R Martins

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