Hemorphins are endogenous peptides belonging to the family of ''noncla
ssical'' or ''atypical'' opioid peptides. They are generated by enzyma
tic hydrolysis of the beta-, kappa-, delta-, or epsilon-chain of the b
lood protein hemoglobin. Originally, the hemorphins were isolated from
enzymatically treated bovine blood. In recent years hemorphin structu
res have been identified as naturally occurring peptides in brain, pla
sma, and cerebrospinal fluid. This article will review recent studies
of rite hemorphins regarding their structures, mechanisms for their re
lease, and their biological actions. A particular emphasis will be dir
ected to their role in exercising human and their clinical relevance.
(C) 1997 John Wiley & Sons, Inc.