Specificity of action on neuropeptides of an endopeptidase from the synaptosomal membranes of guinea pig brain.

@article{Yoshikawa1988SpecificityOA,
  title={Specificity of action on neuropeptides of an endopeptidase from the synaptosomal membranes of guinea pig brain.},
  author={Susumu Yoshikawa and Takako Tashiro and Keitaro Takahashi},
  journal={Journal of biochemistry},
  year={1988},
  volume={104 6},
  pages={1007-10}
}
An endopeptidase was solubilized and highly purified from the synaptosomal membrane fraction of guinea pig brain, and its specificity of action on various neuropeptides was investigated. It hydrolyzed specifically the Pro10-Tyr11 bond of neurotensin and showed a marked specificity toward Pro-X bonds present in the interior parts of various neuropeptides and related peptides. No cleavage, however, was observed at the first and second peptide bonds from the NH2-termini or from the COOH-termini of… CONTINUE READING

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