In vitro metabolism of LVV-Hemorphin-7 by renal cytosol and purified prolyl endopeptidase

The metabolism of LVVH7, an endogenous peptide obtained by cathepsin D hydrolysis of the β chain of hemoglobin, was studied, in vitro, in the presence of cytosol of rat kidney and compared with angiotensin IV. High metabolic activity was found against these two peptides (half life time

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Veröffentlicht in:	Peptides (New York, N.Y. : 1980) N.Y. : 1980), 2003-08, Vol.24 (8), p.1201-1206
Hauptverfasser:	Fruitier-Arnaudin, I., Cohen, M., Coitoux, C., Piot, J.-M.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biochemistry Biochemistry, Molecular Biology Biological and medical sciences Cytosol - metabolism Fundamental and applied biological sciences. Psychology Hemoglobins - metabolism Hemorphin Homogenate In Vitro Techniques Kidney - metabolism Kinetics Life Sciences Male Metabolism Peptide Fragments - metabolism Peptide hydrolysis Prolyl endopeptidase Rats Rats, Wistar Renal cytosol Serine Endopeptidases - metabolism Spectrophotometry, Ultraviolet Subcellular fractions Time Factors Vertebrates: endocrinology
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Beschreibung
Zusammenfassung:	The metabolism of LVVH7, an endogenous peptide obtained by cathepsin D hydrolysis of the β chain of hemoglobin, was studied, in vitro, in the presence of cytosol of rat kidney and compared with angiotensin IV. High metabolic activity was found against these two peptides (half life time
ISSN:	0196-9781 1873-5169
DOI:	10.1016/j.peptides.2003.07.005