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Isolation and primary structure of VIP from sheep brain
1Department of Biochemistry II, Karolinska Institutet, Stockholm, Sweden.
Peptides
|July 1, 1990
Summary
Vasoactive intestinal polypeptide (VIP) shows remarkable conservation across mammals. This study isolated sheep VIP, revealing an amino acid sequence identical to other mammals, confirming its conserved nature.
Area of Science:
- Biochemistry
- Neuroendocrinology
- Comparative Genomics
Background:
- Vasoactive intestinal polypeptide (VIP) is a neuropeptide with crucial physiological roles.
- The amino acid sequence of VIP is known to be highly conserved among various mammalian species.
- Previous research indicated that most mammalian VIP sequences are identical, with the guinea pig as a notable exception.
Purpose of the Study:
- To isolate and determine the primary amino acid sequence of vasoactive intestinal polypeptide (VIP) from sheep brain.
- To compare the sheep VIP sequence with those of other mammalian species.
- To further investigate the conservation of VIP across different mammalian taxa.
Main Methods:
- Isolation and purification of VIP from sheep brain tissue.
- Determination of the primary amino acid sequence of the purified sheep VIP.
- Utilized bioassays and VIP receptor assays to guide purification and confirm biological activity.
Main Results:
- The amino acid sequence of the isolated sheep VIP was successfully determined.
- The primary structure of sheep VIP was found to be identical to that of pig, human, ox, rat, rabbit, goat, and dog VIP.
- This finding reinforces the high degree of sequence conservation for VIP in mammals, excluding the guinea pig.
Conclusions:
- Sheep brain VIP shares an identical amino acid sequence with most other studied mammalian VIPs.
- The study confirms the exceptional conservation of the VIP amino acid sequence across a wide range of mammalian species.
- The conserved nature of VIP suggests a critical and evolutionarily stable functional role.