Hemorphins are endogenous peptides belonging to the family of ''nonclassical'' or ''atypical'' opioid peptides. They are generated by enzymatic hydrolysis of the b-, k-, d-, or 1-chain of the blood protein hemoglobin. Originally, the hemorphins were isolated from enzymatically treated bovine blood.
Opioid peptides derived from hemoglobin: Hemorphins
β Scribed by Q. Zhao; I. Garreau; F. Sannier; J. M. Piot
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1997
- Tongue
- English
- Weight
- 428 KB
- Volume
- 43
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Investigation of hemoglobin peptic hydrolysate has revealed the presence of biologically active peptides with affinity for opioid receptors. Two peptides, VV-hemorphin-7 and LVV-hemorphin-7, were resolved by a combination of size exclusion and reversed phase HPLC. A new spectroscopic method based on the second order derivative spectra analysis of aromatic amino acids has been developed. This method allows qualitative and quantitative evaluation of hemorphins generated by peptic hemoglobin hydrolysis. Using this method, a kinetic study of hemorphins appearance has been undertaken. In this paper, we also evidenced the generation of VV-hemorphin-7 from globin by peritoneal macrophages. In regard to this result, the putative physiological role of hemorphins is discussed.
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Here we review the use of combinatorial libraries in opioid receptor assays. Following a brief description of the history of the combinatorial field, methods for the generation of synthetic libraries and the deconvolution of mixture-based libraries are presented. Case studies involving opioid assays
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