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Degradation of Dynorphin-Related Peptides by the Puromycin-Sensitive Aminopeptidase and Aminopeptidase M by Afshin Safavi; Louis B. Hersh is a Neuroscience article available to read on EtoBox.

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Abstract: The degradation of dynorphin‐related peptides by the puromycin‐sensitive aminopeptidase and aminopeptidase M was examined using these peptides as alternate substrate inhibitors. __K__~i~ determinations showed that both aminopeptidases exhibit a higher affinity for longer dynorphin‐related peptides, i.e., __K__~i~ for dynorphin A‐17 = 23–30 n__M__ with the __K__~i~ increasing to 25–50 μ__M__ for the enkephalin pentapeptides. Binding appears dependent not only on peptide length, but also on its sequence. With aminopeptidase M, as the peptide size increases from five to 10 amino acids, __k__~cat~ remains relatively constant; however, as the peptide size increases beyond a decapeptide, __k__~cat~ decreases significantly. With the puromycin‐sensitive aminopeptidase, similar results were obtained except that __k__~cat~ was greatest for the pentapeptide. Thus, if one considers __k__~cat~/__K__~m~ as the relevant kinetic constant for estimating in vivo peptide hydrolysis, these results are consistent with the involvement of aminopeptidase M and the puromycin‐sensitive aminopeptidase in the degradation of extended dynorphin‐related peptides.

Who reads Degradation of Dynorphin-Related Peptides by the Puromycin-Sensitive Aminopeptidase and Aminopeptidase M?

Author

Afshin Safavi; Louis B. Hersh

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0022-3042)

Published

1995

Language

EN

Field

Neuroscience (Life Sciences)