Abstract:
:The insulins of New World hystricomorph rodents exhibit many novel amino acid changes in primary structure when compared with other mammalian insulins. These changes give rise to unusual properties (low potency, failure to self-associate) not shared by other naturally-occurring insulins. We report here on the primary structure, zinc-binding properties and circular dichroism (CD) of porcupine-insulin (Hystrix cristata), the first Old World hystricomorph insulin to be investigated, and discuss the changes in primary structure of the hormone in relation to its properties. Residue B22 is strongly implicated as being responsible for the unusual properties of porcupine insulin.
journal_name
Naturejournal_title
Natureauthors
Horuk R,Blundell TL,Lazarus NR,Neville RW,Stone D,Wollmer Adoi
10.1038/286822a0subject
Has Abstractpub_date
1980-08-21 00:00:00pages
822-4issue
5775eissn
0028-0836issn
1476-4687journal_volume
286pub_type
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