Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Melvin Levine"'
Publikováno v:
Hypertension. 6:374-382
Spleen cells from mice immunized with partially purified hog kidney renin were fused with mouse myeloma cells to produce a stable monoclonal hybridoma cell line that synthesizes an antibody against renin. A single monoclonal antibody was chosen for s
Publikováno v:
Circulation Research. 34:824-827
Two dipeptides, phenylalanylarginine (Phe-Arg) and serylproline (Ser-Pro), are released sequentially from bradykinin by angiotensin-converting enzyme purified from hog lungs; chloride increases the rate of release of both dipeptides. Using an automat
Publikováno v:
The American Journal of Medicine. 60:737-748
The renin-angiotensin system has an important role in maintaining elevated blood pressure levels in certain forms of experimental and human hypertension. Renin, an enzyme produced by the juxtaglomerular cells of the kidney, acts on a protein substrat
Publikováno v:
Analytical Biochemistry. 87:11-18
Renin substrate, angiotensinogen, has been purified from human plasma by methods which permit the processing of large amounts of outdated bank blood. The purified protein is homogeneous by disc gel electrophoresis at pH 9.5. The specific activity of
Publikováno v:
Circulation Research. 37:715-724
An investigation into the mechanism that sustains the blood pressure in chronic one-kidney hypertension in rabbits was made using passive and active immunization with hog kidney extracts containing renin and with angiotensin antagonists. Seven hypert
Publikováno v:
Circulation Research. 39:400-406
The arterial pressure of rabbits with chronic one-kidney hypertension can be lowered to normotensive levels by direct immunization with preparations made from the cortex of hog kidneys. Hypertensive rabbits that are immunized with large amounts of re
Autor:
Melvin Levine, Harold Tarver
Publikováno v:
Journal of Biological Chemistry. 184:427-436
Autor:
John V. Fopeano, Melvin Levine
Publikováno v:
Journal of Biological Chemistry. 202:597-605
Publikováno v:
Analytical Biochemistry. 33:102-113
An automated, continuous-flow method for measuring angiotensin converting enzyme activity has been developed employing the ninhydrin reaction. The method measures the new free amino group produced when angiotensin I is hydrolyzed to angiotensin II an
Publikováno v:
Circulation Research. 31:356-366
Angiotensin-converting enzyme was purified 1500-fold from a homogenate of hog lungs. The purification procedure included fractionation with ammonium sulfate, inactivation of contaminating enzymes at pH 4.7, batch treatment with CM-cellulose, and chro