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Renin affinity chromatography

As we mentioned, the purification of renal renin had presented insurmountable difficulties in the past (8-17). Recently, several special techniques have been devised and applied to this difficult problem, including affinity chromatography using synthetic inhibitor peptides of renin as affinity ligands (17,20). Burton, et al. synthesized specific renin inhibitors for this purpose (21). These synthetic peptides, however, did not possess sufficiently strong affinity for renin to sequester it from a crude kidney extract. [Pg.227]

Figure 7. Chromatographic elution pattern of porcine big-renin (BB), big renin (B) and small renin (S) from a Sephadex G-150 column. The renin preparation obtained after affinity chromatography on a pepstatin-aminobutyl-agarose gel was the starting material. The renin activity (- -) and protein concentration (—) were determined as in Figure 2 and Ref. (60). ... Figure 7. Chromatographic elution pattern of porcine big-renin (BB), big renin (B) and small renin (S) from a Sephadex G-150 column. The renin preparation obtained after affinity chromatography on a pepstatin-aminobutyl-agarose gel was the starting material. The renin activity (- -) and protein concentration (—) were determined as in Figure 2 and Ref. (60). ...
I. Rubin, E. Lauritzen and M. Lauritzen, University of Copenhagen, Denmark, "Purification of Renin from Rat Kidney by Affinity Chromatography Using the Substrate Analogy NH2-Leu-Leu-Val-Tyr-Ser-C00H". [Pg.343]


See other pages where Renin affinity chromatography is mentioned: [Pg.13]    [Pg.1503]    [Pg.158]    [Pg.230]    [Pg.244]    [Pg.245]    [Pg.441]    [Pg.227]   
See also in sourсe #XX -- [ Pg.14 ]




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