Abstract
'New pressor protein' was observed after tryptic activation of human and rat plasma in vitro, which is done conventionally for prorenin measurements. It is potently pressor, heat labile, possesses enzyme activity, and has a relative molecular mass > 30 kDa with isoelectric point(s) 4.7-4.9. New pressor protein equivalent to only 0.01 ml human, or rat, plasma injected intravenously quickly raises systolic blood pressure in 300 g anesthetized, ganglion-blocked, bioassay rats by about 15 mmHg. For unknown reasons, this is potentiated to about 45 mmHg after treatment with angiotensin I converting enzyme inhibitors (such as captopril and enalapril). New pressor protein activity in rats remains normal 24 h after bilateral nephrectomy, suggesting that it has an extrarenal origin and, furthermore, excluding the possibility of an association with renin-angiotensin system. Systolic blood pressure elevation is greater than the diastolic one, implicating cardiotonic effects. Human plasma new pressor protein was purified using standard biochemical techniques and its N-terminal sequence (19 residues) found to be homologous with the beta factor XIIa fragment of coagulation factor XII. This was supported by demonstrating inhibition of new pres...Continue Reading
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Citations
Jan 6, 2012·Clinical Science·Peter C PapageorgiouJohn S Floras
Oct 25, 2003·American Journal of Physiology. Heart and Circulatory Physiology·Peter C PapageorgiouDaniel H Osmond
May 29, 2004·Journal of Hypertension·Akis A AmfilochiadisDaniel H Osmond
Dec 20, 2007·Journal of Hypertension·Akis A AmfilochiadisJohn S Floras