Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Prolylendopeptidase Inhibitory Activity of a Glial Fibrillary Acidic Protein Fragment and Other Proline-rich Peptides
Susumu MARUYAMATakashi OHMORITatsuyoshi NAKAGAMI
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JOURNAL FREE ACCESS

1996 Volume 60 Issue 2 Pages 358-359

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Abstract
The brain prolylendopeptidase (PEP) inhibitory activity of syn-thetic peptides related to the bovine brain-derived PEP inhibitor, GFAP-(38-55) (MPPPLPARVDFSLAGALN), was investigated. Homologous peptides such as MPPPLPTRVDFSLAGALN (human type) and MTPPLPARVDFSLAGALN (mouse type) also inhibited PEP. Among various synthetic fragments of GFAP-(38-55), only MPPPLP had a Ki essentially the same as that of GFAP-(38-55). Similar synthetic proline-rich peptides such as synapsin fragments and SH3 domain-binding peptides had more or less inhibitory activity.
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