Structure of equine corticotropin releasing factor.

This research investigates the structure and sequence of a 41 amino acid peptide called equine corticotropin releasing factor, which is likely identical to the human version.

Methodology

• The researchers began by isolating the peptide from 70 equine hypothalamus tissues using methanol extraction, immunoaffinity chromatography, and a single step of reverse phase High Performance Liquid Chromatography (HPLC).
• The amino acid sequence was then determined using gas phase sequence analysis, a technique that provides high sensitivity and accuracy for peptide sequencing.

Findings

• The study found that the equine corticotropin releasing factor likely has a carboxyl terminal amidation. This was demonstrated by the similar retention times for both the equine and human versions of the factor when subjected to reverse phase HPLC at pH 8.
• The researchers were able to identify the probable structure of the equine corticotropin releasing factor. The sequence comprises 41 amino acids, as outlined in the article.

Implications

• The purified equine peptide was tested against the human corticotropin releasing factor in an in vitro bioassay and in a human plasma binding protein assay. The equine factor showed equipotency with its human counterpart, meaning it could potentially have similar biological effects in horses as the human factor does in humans.
• This finding may have important implications for better understanding how this factor functions in equines and could have potential applications in veterinary medicine, particularly for stress-related disorders where corticotropin releasing factor plays a major role.