By Leonard T. Skeggs, Frederic E. Dorer, Joseph R. Kahn, Kenneth E. Lentz (auth.), Irvine H. Page M.D., F. Merlin Bumpus Ph.D. (eds.)
The historical past of arterial high blood pressure is either lengthy and brief; lengthy, when you consider that shiny (1827) first comparable hardness of the heart beat to hardness of the kidneys and hyper. trophy of the center; brief in that sleek study begun within the past due twenties. so much of what we all know of those ailments has been came across long ago fifty years. the trendy tale must have started in 1897 whilst an extract of kidney used to be proven to be pressor. yet little was once performed with wisdom until eventually approximately 1929 while the connection of this kidney extract referred to as "renin" to high blood pressure was once pos· tulated. The pressor results have been, in spite of the fact that, not like such a lot of these noticeable with sub· stances corresponding to epinephrine or vasopressin. Plasma was once required for motion of renin and the energetic substance protein. In 1939, it was once proven that renin used to be now not in itself a pressor substance yet relatively a proteolytic enzyme which produced a robust pressor substance performing on a substrate synthesized by way of the liver. Later it was once famous that the 1st definable step after the formation of this peptide used to be cleaving of the decapeptide which had very little demonstrable task, with lack of amino acids to shape the octapeptide referred to as "angiotensin". inside of a decade synthesis used to be completed which made the substance to be had for world·wide study.
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Extra resources for Angiotensin
I across an organ are compared (NG and VANE, 1968) an overall disappearance of activity occurs, amounting to 40 to 50 % in the head, 60 to 90 % in the hind legs and 80 to 90 % in the kidney. This overall inactivation of Ang. I in one passage through the different vascular beds is similar to that found for Ang. II and since tissue angiotensinases include aminopeptidases and/or endopeptidases (LEARY and LEDINGHAM, 1972) it is possible that the same enzymes degrade both Ang. I and Ang. II, which only differ structurally at the carboxy end of the molecule.
Results obtained with these techniques in general correspond to those obtained in vivo, so they will be presented together. a) Lung NG and VANE (1967) showed that in vivo, Ang. I was converted to Ang. II in the 3 to 5 sec that it takes for blood to pass through the pulmonary circulation (Fig. 2). Conversion of Ang. , 1971 (1)]. Such an experiment is illustrated in Fig. 3 (from AIKEN and VANE, 1970). Guineapig lungs were perfused with Krebs' solution; the lung effluent then superfused a rat-colon preparation which detected Ang.
I. Preparation and assay of human renin, human hypertensinogen, and hypertensin. J. clin. Invest. 24, 62 (1945). ELLIOTT, D. , PEART, W. : The amino acid sequence in a hypertensin. Biochem. J. 66, 246 (1957). FASCIOLO, J. , HOUSSAY, B. , TAQUINI, A. pressure raising secretion of the ischaemic kidney. J. PhysioI. ) 94, 281 (1938). FERRIS, T. , MULROW, P. : Rabbit uterus as a source of renin. Amer. J. Physiol. 212,698 (1967). , NAHMOD, V. : In vitro production of angiotensin I by renal glomeruli.
Angiotensin by Leonard T. Skeggs, Frederic E. Dorer, Joseph R. Kahn, Kenneth E. Lentz (auth.), Irvine H. Page M.D., F. Merlin Bumpus Ph.D. (eds.)