Beta-endorphin. Binding activity of synthetic analogs with various chain lengths in neuroblastoma x glioma NG108-15 cell membranes.

Abstract

Inhibition of binding of beta h-endorphin or Leu-enkephalin by beta h-endorphin analogs of various chain lengths in memmbrane preparations of the neuroblastoma x glioma NG108-15 cells has been investigated. The removal of even a single residue from the C-terminus results in the inability of the resulting peptide to completely displace beta h-endorphin. In addition, the proportion of nondisplaceable binding increases with decreasing chain length.

• Authors: R G Hammonds Jr, P Ferrara, C H Li
• Journal: International journal of peptide and protein research (Int J Pept Protein Res) Vol. 24 Issue 6 Pg. 597-9 (Dec 1984) ISSN: 0367-8377 [Print] Denmark
• PMID: 6099337 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Endorphins
• Receptors, Opioid
• Enkephalin, Leucine
• beta-Endorphin

Topics

• Animals
• Cell Membrane (metabolism)
• Endorphins (metabolism)
• Enkephalin, Leucine (metabolism)
• Glioma
• In Vitro Techniques
• Kinetics
• Neuroblastoma
• Rats
• Receptors, Opioid (metabolism)
• Structure-Activity Relationship
• beta-Endorphin