ArticleReassessment of plasma angiotensins measurement: Effects of protease inhibitors and sample handling procedures
References (33)
- et al.
Identification of angiotensin-(1–7) in rat brain—evidence for differential processing of angiotensin peptides
J. Biol. Chem.
(1989) - et al.
Characterization by high performance liquid chromatography of angiotensin peptides in the plasma and cerebrospinal fluid of the dog
Peptides
(1987) - et al.
Processing of angiotensin peptides by NG108-15 neuroblastoma × glioma hybrid cell line
Peptides
(1990) - et al.
Measurement of immunoreactive angiotensin peptides in rat tissue: Some pitfalls in angiotensin II analysis
Anal. Biochem.
(1988) - et al.
Characterization of aminopeptidase B: Substrate specificity and affector studies
Arch. Biochem. Biophys.
(1966) - et al.
In vitro renin inhibition to prevent generation of angiotensins during determination of angiotensin I and II
Life Sci.
(1988) - et al.
Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase
Peptides
(1984) - et al.
A human platelet angiotensin I-processing system; identification of components and inhibition of angiotensin-converting enzyme by product
J. Biol. Chem.
(1985) - et al.
Purification by affinity chromatography using amastatin and properties of aminopeptidase A from pig kidney
Biochem. Biophys. Acta
(1980) - et al.
Characterization of proline endopeptidase from rat brain
Biochemistry
(1980)
Enzyme inhibitors in relation to cancer therapy
J. Antibiot.
Degradation of low-molecular-weight opioids by vascular plasma membrane aminopeptidase M
Biochem. Biophys. Acta
Simultaneous radioimmunoassay of six angiotensin peptides in arterial and venous plasma of man
J. Hypertens.
Soluble metalloendopeptidase from rat brain action of enkephalin-containing peptides and other bioactive peptides
Endocrinology
Proline endopeptidase in human muscle
Biochem. Soc. Transact.
Leucine aminopeptidase and other N-terminal exopeptidases
Cited by (82)
Newly developed radioimmunoassay for Human Angiotensin-(1–12) measurements in plasma and urine
2021, Molecular and Cellular EndocrinologyCitation Excerpt :Furthermore, the anti-Ang-(1–12) antibody does not cross-react with any closely related angiotensin peptides [Ang I, Ang-(1–9), Ang II and Ang-(1–7)] at endogenous concentrations reported in human plasma and urine (Lijnen et al., 1978; Cohall et al., 2015; Katsurada et al., 2007; Kobori et al., 2009; Saito et al., 2009; Juretzko et al., 2017). Using this polyclonal antibody, the assay conditions for Ang-(1–12) measurements were identified in individual blood samples drawn from five adult volunteers (3 males and 2 females, age range 20–55 years) and collected with and without a previously reported inhibitor cocktail (Brosnihan and Chappell, 2017; Kohara et al., 1991; Chappell, 2016a). Similarly, collected spot urine samples were processed in the presence and absence of HCl (described in Methods section).
Fetal and postnatal zinc restriction: sex differences in the renal renin-angiotensin system of newborn and adult Wistar rats
2020, Journal of Nutritional BiochemistryInterference by o-phenanthroline in the radioimmunoassay of angiotensin II in small volume blood samples
2012, Clinical BiochemistryCitation Excerpt :Extracted buffer samples had slightly higher concentrations than non extracted buffer samples (Table 1), presumably due to higher concentrations of o-phenanthroline in the extract. Previous studies investigating the effects of o-phenanthroline on measurement of Ang II commonly used radioactive Ang II to look at its degradation profile [5,6]. Whereas those studies were capable of detecting direct effects of o-phenanthroline on degradation of Ang II, they would not detect interference by this compound in the assay.