Abstract
Abstract The stability of human growth hormone to acid, alkali, and urea has been evaluated by fluorescence, absorption, and circular dichroism spectroscopy. In accord with previous studies on other growth hormones and prolactins, similar molecular transitions were observed although small shifts in parameters were found among the different proteins. It is of interest to find such a resemblance in properties between human growth hormone and ovine prolactin since the number of residues occupying identical positions is less than 20% and the longest identical sequence is a tripeptide.
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