On a domain structure of colicin E1. A COOH-terminal peptide fragment active in membrane depolarization

A prolonged digestion of colicin E1 with dilute trypsin results in the generation of a trypsin-resistant peptide fragment of the colicin which is approximately one-third of the molecule. The amino acid composition of the fragment, Mr = 20,000, is more nonpolar in nature than the colicin, with the ma...

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Veröffentlicht in:	The Journal of biological chemistry 1982-04, Vol.257 (7), p.3857-3863
Hauptverfasser:	Dankert, J R, Uratani, Y, Grabau, C, Cramer, W A, Hermodson, M
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - analysis Biological Transport Cell Membrane - physiology Circular Dichroism Colicins - metabolism Dimyristoylphosphatidylcholine Escherichia coli - physiology Kinetics Liposomes Molecular Weight Peptide Fragments - pharmacology Phosphatidylcholines Proline - metabolism Trypsin - metabolism
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