Literature DB >> 11212317

A C-terminally elongated form of PHI from porcine intestine.

E Eriste1, A Norberg, V Bonetto, D Nepomuceno, T W Lovenberg, R Sillard, H Jörnvall.   

Abstract

A C-terminally elongated form of peptide histidine isoleucine amide (PHI) was isolated from porcine intestine based on its effect on cAMP production in IMR-32 cells. The structure was determined by amino acid sequence analysis of tryptic fragments and by mass spectrometry. The peptide has 42 amino acid residues like those described from human, rat and mouse, but the amino acid sequence of the C-terminal extension of pig PHI is unique. Unlike the other peptides, it has a C-terminal Ala and it differs at five positions from the human form and at six positions from the rat form, while the human and the rat forms differ by only two substitutions. To avoid confusion arising from different C-terminal residues, a unifying nomenclature is proposed: PHI-27 for the hormone and PHI-42 for the elongated product.

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Year:  1999        PMID: 11212317     DOI: 10.1007/s000180050464

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  1 in total

1.  Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidase.

Authors:  Peep Palumaa; Liina Kangur; Anastassia Voronova; Rannar Sillard
Journal:  Biochem J       Date:  2004-08-15       Impact factor: 3.857

  1 in total

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