Purification of an Aminopeptidase Preferentially Releasing N-terminal Alanine from Cucumber Leaves and Its Identification as a Plant Aminopeptidase N
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Purification and properties of an alanine aminopeptidase from camel liver
Article history: Received on: 03/10/2016 Accepted on: 20/01/2017 Available online: 30/05/2017 Alanine aminopeptidase is purified from camel liver to homogeneity and designated CLAAP. The purification procedure involved anion exchange chromatography on DEAE-cellulose column and gel filtration chromatography on Sephacryl S-300 column. The specific activity of CLAAP is increased to 9.9 folds over ...
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The nucleotide sequence of the pepN gene from Lactococcus lactis encoding a zinc-metallo aminopeptidase has been determined. The open reading frame of 2,538 base pairs encodes a protein with a calculated M(r) of 95,368, which agrees with the apparent M(r) of 95,000 of the gene product which was identified by polyclonal antibodies raised against the purified aminopeptidase. The amino acid sequen...
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An aminopeptidase from Escherichia coli has been purified to homogeneity and crystallized. This peptidase is responsible for about 65% of the hydrolytic activity found in crude extracts toward the substrate methionylalanylserine. It resembles the so-called leucine arninop!ptidase of hog kidney in several respects, including size, metal requirements, and peptide specificity. Evidence based on su...
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The aminopeptidase which had been shown to be present in Mycoplasma salivarium was found to be associated with the cell membranes of the organism. The enzyme was solubilized in water by papain digestion of the membranes pretreated with Triton X-100 and purified approximately 130-fold by ion-exchange chromatography on DEAE-Sephadex A-50, affinity chromatography on L-leucylglycine-AH-Sepharose 4B...
متن کاملPurification and properties of an aminopeptidase from Escherichia coli.
An aminopeptidase from Escherichia coli has been purified to homogeneity and crystallized. This peptidase is responsible for about 65% of the hydrolytic activity found in crude extracts toward the substrate methionylalanylserine. It resembles the so-called leucine arninop!ptidase of hog kidney in several respects, including size, metal requirements, and peptide specificity. Evidence based on su...
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ژورنال
عنوان ژورنال: Bioscience, Biotechnology, and Biochemistry
سال: 2001
ISSN: 0916-8451,1347-6947
DOI: 10.1271/bbb.65.2802