Purification and properties of an aminopeptidase from Treponema phagedenis (Reiter strain)

An aminopeptidase was higly purified from a cellular extract of Treponema phagedenis (Reiter strain) by ammonium sulfate precipitation and successive chromatography on Sepharose 6B, DEAE-Sepharose CL-6B and CM-Sepharose CL-6B. The molecular weight of the enzyme was 74,500. The enzyme was stable in t...

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Bibliographic Details
Published in:Current microbiology 1985-01, Vol.12 (5), p.283-288
Main Authors: TAKAHASHI, T, ASARI, K, SATO, N, YAMAYA, S.-I, SUGAHARA, T
Format: Article
Language:English
Subjects:
aminopeptidase
Bacteriology
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Metabolism. Enzymes
Microbiology
Treponema phagedenis
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Summary:An aminopeptidase was higly purified from a cellular extract of Treponema phagedenis (Reiter strain) by ammonium sulfate precipitation and successive chromatography on Sepharose 6B, DEAE-Sepharose CL-6B and CM-Sepharose CL-6B. The molecular weight of the enzyme was 74,500. The enzyme was stable in the pH region 5.0-7.0 and up to 50 degree C. The optimal pH, ionic strength, and temperature were pH 7.9-8.0, I 0.13, and 37 degree C, respectively. Co super(2+) was essential for the enzyme activity with an optimal concentration of 0.3 mM, and EDTA and such divalent cations as Hg super(2+), Cu super(2+), Zn super(2+) pB super(2+), Sn super(2+), and Cd super(2+) were inhibitory against the Co super(2+)-activated enzyme. The enzyme exhibited a preference for hydrophobic residues as well as Arg in the N-terminal position and cleaved in the order of Tyr > Trp > Phe > Leu > Arg > Ala > His, Met, and Ser, but did not cleave the other amino acids including Pro, Glu, Asp, and Lys.
ISSN:0343-8651
1432-0991
DOI:10.1007/BF01567979