1981
DOI: 10.1042/bj1970085
|View full text |Cite
|
Sign up to set email alerts
|

Abstract: Highly purified rabbit brain endo-oligopeptidase A injected into goats produced, after 60 days of immunization, antisera that specifically inhibit purified rabbit brain endo-oligopeptidase A. An immunoreactive kininase having the same specificity as rabbit brain endo-oligopeptidase A for bradykinin was detected in several rabbit tissues. The highest amount of this immunoreactive kininase was found in the 25000 g supernatant fraction (S fraction) of heart, liver, skeletal muscle, ovary, brain and testis homogen… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3

Citation Types

0
5
0

Year Published

1981
1981
2013
2013

Publication Types

Select...
6
3

Relationship

1
8

Authors

Journals

citations
Cited by 11 publications
(5 citation statements)
references
References 20 publications
0
5
0
Order By: Relevance
“…Previous reports from our laboratory indicated that, when bradykinin is incubated with purified brain endooligopeptidase A or B, the major peptides formed are Arg1 -* Phe5 and Arg1 -* Pro7, respectively (Oliveira et al, 1976). Since these fragments are slowly degraded by brain peptidases present in tissue homogenate (Cicilini et al, 1977;Coelho et al, 1981), the amount of Arg1 -* Phe5 and Arg1 -* Pro7 formed when bradykinin is incubated with enzyme preparations was used to evaluate the relative activity of brain endooligopeptidases A and B, respectively, present in the early stage of enzyme purification. The quantitative recovery of bradykinin products formed by the action of brain peptidases clearly shows that purified brain endooligopeptidases A and B are free from any other peptidases acting on bradykinin or on its products.…”
Section: Discussionmentioning
confidence: 98%
See 1 more Smart Citation
“…Previous reports from our laboratory indicated that, when bradykinin is incubated with purified brain endooligopeptidase A or B, the major peptides formed are Arg1 -* Phe5 and Arg1 -* Pro7, respectively (Oliveira et al, 1976). Since these fragments are slowly degraded by brain peptidases present in tissue homogenate (Cicilini et al, 1977;Coelho et al, 1981), the amount of Arg1 -* Phe5 and Arg1 -* Pro7 formed when bradykinin is incubated with enzyme preparations was used to evaluate the relative activity of brain endooligopeptidases A and B, respectively, present in the early stage of enzyme purification. The quantitative recovery of bradykinin products formed by the action of brain peptidases clearly shows that purified brain endooligopeptidases A and B are free from any other peptidases acting on bradykinin or on its products.…”
Section: Discussionmentioning
confidence: 98%
“…Furthermore, the antibody directed against endooligopeptidase A did not cross-react with endooligopeptidase B and vice versa. The antibody has proved to be a useful tool for determining the presence of endooligopeptidase A in peripheral tissues (Coelho et al, 1981).…”
Section: Discussionmentioning
confidence: 99%
“…It has been postulated that enzymes that participate in neuropeptide processing or degradation should be found in secretory granules and in cytoplasmic membranes, respectively (Loh and Parish, 1987;Turner et al, 1987). Thus, an enzyme such as EC 3.4.22.19, which is predominantly associated with the soluble protein fraction of brain homogenates (Camargo et al, 1973;Cicilini et al, 1977;Coelho et al, 1981), would not be a suitable candidate for participating in neuropeptide metabolism. However, in the present study, we showed a significant amount of activity in the crude mitochondria1 fraction, including in synaptosomal membranes.…”
Section: Discussionmentioning
confidence: 99%
“…Although endo-oligopeptidase A activity can possibly be detected with Pz-peptidase substrate (Tisljar et al, 1989), we would strongly suggest that the use of either bradykinin or a more selective chromogenic substrate for endo-oligopeptidase A such as QF-ERP7 [o-aminobenzoyl-Gly-Gly-Phe-Leu-Arg-Arg-Val- (2,4-dinitrophenyl)ethylenediaminel, a quenched fluorescent enkephalin-related peptide (Juliano et al, 1990) to distinguish this enzyme from other soluble endopeptidases present in the cytosol of nervous tissue. This suggestion arises from the observation that the addition of monospecific antibodies raised against purified endo-oligopeptidase A to brain cytosol completely prevent the hydrolysis of the F5-S6 bond of bradykinin (Coelho et al, 1981). Similar results were obtained when QF-ERP7 instead of bradykinin was used as a substrate (Juliano et al, 1990).…”
mentioning
confidence: 73%