The Amino‐Acid Sequence of the Three Smallest CNBr Peptides from p‐Hydroxybenzoate Hydroxylase from Pseudomonas fluorescens
Autor: | Jan Hofsteenge, Henk J. Bak, Johan M. Vereijken, Jaap J. Beintema |
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Jazyk: | angličtina |
Rok vydání: | 1980 |
Předmět: |
chemistry.chemical_classification
Edman degradation biology Chemical Phenomena Homoserine Pseudomonas fluorescens biology.organism_classification Cleavage (embryo) 4-Hydroxybenzoate-3-Monooxygenase Biochemistry Peptide Fragments Amino acid Mixed Function Oxygenases N-terminus chemistry.chemical_compound Chemistry Enzyme chemistry Amino Acid Sequence Cyanogen Bromide Peptide sequence |
Zdroj: | European Journal of Biochemistry, 113(1), 151-157. Blackwell Publishing Ltd |
ISSN: | 0014-2956 |
Popis: | After CNBr cleavage of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, five peptides and free homoserine were isolated (see preceding paper in this journal). The amino acid sequences of the three smallest peptides, viz. CB3, CB4 and CB5, were determined by automated Edman degradation and analysis of enzymatic subdigests. These peptides form a continuous stretch of 110 residues from the N terminus: (Formula: See Text). |
Databáze: | OpenAIRE |
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