[A membrane-bound alanine aminopeptidase from Acinetobacter calcoaceticus. 1. Isolation and purification of the enzyme].
The alanine aminopeptidase of Acinetobacter calcoaceticus was found to be bound to the inner membranes only. The enzyme was solubilized by Triton X-100 and purified approximately 480-fold by gel filtration and affinity chromatography on alanine methyl ketone-AH-Sepharose 4B. The purified alanine aminopeptidase has a molecular mass of 212 kDa, estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme selectively catalyses the hydrolysis of N-terminal alanine residues of peptides. The enzyme is inhibited by p-hydroxy-mercuribenzoate, 1,10-phenanthroline, and puromycin, but was activated by CO2(+)-ions.
Jahreis
G
G
Institut für Biochemie, Bereich Medizin, Martin-Luther-Universität Halle-Wittenberg.
Sorger
H
H
Aurich
H
H
D000150:Acinetobacter / Q000201:enzymology*; D000626:Aminopeptidases / Q000302:isolation & purification*; D018826:CD13 Antigens; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D008566:Membranes / Q000201:enzymology; D008970:Molecular Weight; D017830:Octoxynol; D011092:Polyethylene Glycols; D011485:Protein Binding
D011092:Polyethylene Glycols; D017830:Octoxynol; D000626:Aminopeptidases; D018826:CD13 Antigens
Eine membrangebundene Alaninaminopeptidase aus Acinetobacter calcoaceticus. 1. Isolierung und Reinigung des Enzyms.