Download Angiotensin by Leonard T. Skeggs, Frederic E. Dorer, Joseph R. Kahn, PDF

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.)

ISBN-10: 3642656021

ISBN-13: 9783642656026

The heritage of arterial high blood pressure is either lengthy and brief; lengthy, seeing that vivid (1827) first comparable hardness of the heartbeat to hardness of the kidneys and hyper. trophy of the guts; brief in that sleek study all started within the overdue twenties. such a lot of what we all know of those ailments has been chanced on long ago fifty years. the trendy tale must have started in 1897 while an extract of kidney was once proven to be pressor. yet little used to be performed with wisdom till approximately 1929 whilst the connection of this kidney extract known as "renin" to high blood pressure was once pos· tulated. The pressor results have been, besides the fact that, in contrast to such a lot of these noticeable with sub· stances similar to epinephrine or vasopressin. Plasma used to be required for motion of renin and the energetic substance protein. In 1939, it was once proven that renin used to be no longer in itself a pressor substance yet really a proteolytic enzyme which produced a strong pressor substance performing on a substrate synthesized through the liver. Later it was once famous that the 1st definable step after the formation of this peptide was once 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 on hand for world·wide study.

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SKEGGS, L. , KAHN, J. , SHUMWAY, N. : The isolation and assay of hypertensin from blood. J. expo Med. 95,241 (1952). SKEGGS, L. , LENTZ, K. , KAHN, J. R: The purification and partial characterization of several forms of hog renin substrate. J. expo Med. 118, 73 (1963). SKEGGS, L. , LENTZ, K. , KAHN, J. , DORER, F. : Pseudorenin. A new angiotensin-forming enzyme. Circulat. Res. 25, 451 (1969). 16 L. T. : The Biological Production of Angiotensin SKEGGS, L. , LENTZ, K. , KAHN, J. : Studies on the preparation and properties of renin.

In cell-free homogenates of the twenty-five tissues of rat which they studied (Table 1) they found detectable converting-enzyme activity in all but the gastrocnemius muscle and liver. In those which demonstrated sufficient activity, they characterized the enzyme further by The Fate of Angiotensin I 23 showing that (a) it was inhibited by the pentapeptide inhibitor of converting enzyme, (b) the activity was chloride-dependent and (c) the activity was stimulated by cobalt ions. Three tissues were outstanding for their converting-enzyme activity; lung, testis and epididymis.

1971 (1)]. In most of these instances the substances released have been identified as prostaglandin or prostaglandin-like. The chick rectum readily distinguishes between angiotensin and prostaglandins, for it does not react to Aug. I or Aug. II, but is strongly contracted by the commonly released prostaglandins such as E I , E2 and F 2"'. It is for this reason that we always include a chick rectum in our parallel-bioassay system. TURKER et ai. [1971 (1)] did not use this preparation in their assay system, so it is not known whether the rat colon contracting substance released from lungs by Aug.

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