Acylpeptide hydrolase activity from erythrocytes |
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| Authors: | W M Jones J M Manning |
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| Institution: | 3. High Pressure and Synchrotron Radiation Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai, Maharashtra 400085, India;5. Food Technology Division, Bhabha Atomic Research Centre, Trombay, Mumbai, Maharashtra 400085, India;4. School of Biochemistry, Devi Ahilya University, Indore 452001, India;1. University of Idaho, Moscow, ID, 83844, USA;2. Idaho National Laboratory, Idaho Falls, ID, 83415, USA;3. Center for Advanced Energy Studies, Idaho Falls, ID, 83401, USA |
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| Abstract: | Acylpeptide hydrolase, which cleaves the NH2-terminal acetylated or formylated amino acid from a blocked peptide, has been purified to apparent homogeneity from human erythrocytes. The enzyme catalyzes the hydrolysis of a diverse number of peptides and displays different pH optima for certain substrates in doing so. Zinc inhibits to the same extent the hydrolysis of both the most efficient and the least efficient substrates. This enzyme may play a pivotal role in the processing of polypeptide chains during biosynthesis. |
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