Properties of an Escherichia coli rhodanese.
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چکیده
منابع مشابه
Purification 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...
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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Background & Objectives: Antisense peptide nucleic acids (PNA) that target growth essential genes show potent bactericidal properties without cell lysis. We considered the possibility that whether PNA treatment influence the bacteria total nucleic acids content and apply approach to develop a new delivery system to Dendritic cells (DCs). DCs are the most potent antigen presenting cells in th...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)48283-x