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Characterization of the pro-aminopeptidase from Aeromonas caviae T-64

Bioscience, Biotechnology, and Biochemistry

Feb 1, 2001

Z Z ZhangKyozo Hayashi

PMID: 11302179

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Abstract

The pro-aminopeptidase from Aeromonas caviae T-64 (pro-apAC) had maximal activity at 60 degrees C and was more stable than mature apAC at temperature up to 65 degrees C for 1 hour. The pH stability of pro-apAC ranged from 4.0 to 8.0, which is broader than the range for the mature apAC. ...read more

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Bestatin, (L-Leu)-(S-(R*,R*))-isomer
Aeromonas punctata (organism)
Phenanthrolines
Substrate Specificity
1,10-phenanthroline, zinc salt
Hydrogen-Ion Concentration
Aminopeptidase
Enzyme Stability
Oligopeptides
Leucine
Paper Details
References

Characterization of the pro-aminopeptidase from Aeromonas caviae T-64

Bioscience, Biotechnology, and Biochemistry

Feb 1, 2001

Z Z ZhangKyozo Hayashi

PMID: 11302179

DOI:

Abstract

The pro-aminopeptidase from Aeromonas caviae T-64 (pro-apAC) had maximal activity at 60 degrees C and was more stable than mature apAC at temperature up to 65 degrees C for 1 hour. The pH stability of pro-apAC ranged from 4.0 to 8.0, which is broader than the range for the mature apAC. ...read more

Mentioned in this Paper

Bestatin, (L-Leu)-(S-(R*,R*))-isomer
Aeromonas punctata (organism)
Phenanthrolines
Substrate Specificity
1,10-phenanthroline, zinc salt

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