Kinetic of in vitro generation of some hemorphins: early release of LVV-hemorphin-7, precursor of VV-hemorphin-7

Neuropeptides. 1996 Feb;30(1):1-5. doi: 10.1016/s0143-4179(96)90047-5.

Abstract

Bovine globin has been hydrolysed by pepsin to different degrees of hydrolysis. Analysis of the hydrolysates, by reversed-phase high-performance liquid chromatography (RP-HPLC), shows the release of LVV- and VV-hemorphin-7. LVV-hemorphin-7 was the first generated, at a degree of hydrolysis (DH), as low as 4%. In contrast, VV-hemorphin-7 was produced later. Our study clearly shows that VV-hemorphin-7 is issued directly from LVV-hemorphin-7, since this later completely disappeared during hydrolysis. This work allows us to suggest a possible pathway for in vivo hemorphins appearance.

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Cattle
  • Chromatography, High Pressure Liquid
  • Globins / chemistry
  • Hemoglobins / chemistry*
  • Hydrolysis
  • Kinetics
  • Peptide Fragments / chemistry*
  • Spectrophotometry, Ultraviolet

Substances

  • Amino Acids
  • Hemoglobins
  • Peptide Fragments
  • LVV-hemorphin-7
  • VV-hemorphin-7
  • Globins