Abstract
The current methods used for plasma total kininogen determination are mostly based on bioassay on smooth muscle of the bradykinin activity of a trypsin hydrolysate of denaturated plasma. The accuracy of this principle is, however, open to question, since it is known that some trypsin liberated plasma peptides are capable of potentiating the effect of bradykinin on smooth muscle. The interference caused by this potentiating factor in plasma kininogen determination was verified and quantitated in bioassay on the rat uterus in vitro. It has been shown that the bradykinin activity of the crude trypsin hydrolysate is considerably overestimated (by a factor of 1.9 on average in the present series) if the potentiating peptides are not removed. This can be easily accomplished by ion exchange chromatography, with a loss of about 10% of the bradykinin activity. The mean plasma kininogen content of 10 healthy human subjects, determined by using trypsin hydrolysates purified in this way, was found to be 3.8 μg/ml (S.D. 0.67) in bradykinin equivalents.
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