A human serine endopeptidase, purified with respect to activity against a peptide with phosphoserine in the P1' position, is apparently identical with prolyl endopeptidase

The present work describes the detection, purification, and characterization of a serine endopeptidase with preference for a phosphoserine in the P1‘ position of the substrate. During probing for the enzyme in crude extracts, as well as during its 64,000-fold purification, 32P-labeled guanidovaleryl...

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Veröffentlicht in:	The Journal of biological chemistry 1991-02, Vol.266 (6), p.3827-3834
Hauptverfasser:	Rosén, J, Tomkinson, B, Pettersson, G, Zetterqvist, O
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Autoradiography Biological and medical sciences Chromatography, DEAE-Cellulose Electrophoresis, Polyacrylamide Gel Endopeptidases - chemistry Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Humans Hydrolases Liver - enzymology Molecular Sequence Data Phosphoserine - chemistry Prolyl Oligopeptidases Protease Inhibitors - pharmacology Rats Serine Endopeptidases - chemistry Substrate Specificity
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