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The neuropeptide head activator loses its biological acitivity by dimerization.

Authors
  • H Bodenmüller
  • E Schilling
  • B Zachmann
  • H C Schaller
Publication Date
Aug 01, 1986
Source
PMC
Keywords
Disciplines
  • Biology
License
Unknown

Abstract

On molecular sieve columns the neuropeptide head activator elutes at two distinct positions corresponding to apparent mol. wts of 700 and 1400 daltons. The low mol. wt component is stable only under high ionic conditions and represents the monomeric state of the head activator. Only this form is biologically active. The higher mol. wt component, which is reapidly formed under physiological conditions, is the dimeric head activator and is biologically inactive. We suggest that this dimerization is of biological relevance as a mechanism for inactivation of neuropeptides.

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