TY - JOUR

T1 - A comparison of the properties of renin isolated from pig and rat kidney

AU - Lauritzen, M.

AU - Damsgaard, J. J.

AU - Rubin, I.

AU - Lauritzen, E.

PY - 1976/1/1

Y1 - 1976/1/1

N2 - On isoelectric focusing, renin from rat kidneys showed three activity peaks with pI values at pH 5.0, 5.2 and 5.4 after a purification procedure involving differential centrifugation, acidification, chromatography on Sephadex G 75 and dialysis. The preparation (purified 140 fold) was compared with a crude kidney extract in the absence and presence of 3 (M) urea by isoelectric focusing. The pattern of activity distribution was confirmed by these experiments and the content of isoenzymes in the three groups calculated. Pig renin was prepared and compared with rat renin with regard to molecular weight, acid activation, behavior on isoelectric focusing, immunogenicity and substrate affinity. Extracts of rat kidney contained multiple forms of renin with mol wt. between 39 000 and 42 000, whereas active pig renin had an approximate mol. wt. of 40 000. Acidification of rat renal extracts did not increase the activity of renin, indicating the absence of an inactive form of renin in rat kidneys, whereas pig renin was activated by this procedure. Pig renin has isoelectric points at pH 4.6, 4.8, 5.05 and 5.2, significantly lower than for rat renin. The isoenzymes from the two species had no antigenicity in common, as shown by crossed immunoelectrophoresis or rocket immunoelectrophoresis. The Michaelis constants for pig and rat renin were in the same range, 1x10-6M, when rat renin substrate was used. The relative content of rat isoenzyme with pI in the pH ranges 4.9-5.1, 5.1-5.3 and 5.3-5.5 was approx. 20, 27 and 53% respectively. Purified pig renin prepared in two different ways had isoenzymes with pI in the pH regions 4.5-4.7, 4.7-4.9, 4.9-5.05 and 5.05-5.20 in the approximate proportions 14, 24, 28 and 29%.

AB - On isoelectric focusing, renin from rat kidneys showed three activity peaks with pI values at pH 5.0, 5.2 and 5.4 after a purification procedure involving differential centrifugation, acidification, chromatography on Sephadex G 75 and dialysis. The preparation (purified 140 fold) was compared with a crude kidney extract in the absence and presence of 3 (M) urea by isoelectric focusing. The pattern of activity distribution was confirmed by these experiments and the content of isoenzymes in the three groups calculated. Pig renin was prepared and compared with rat renin with regard to molecular weight, acid activation, behavior on isoelectric focusing, immunogenicity and substrate affinity. Extracts of rat kidney contained multiple forms of renin with mol wt. between 39 000 and 42 000, whereas active pig renin had an approximate mol. wt. of 40 000. Acidification of rat renal extracts did not increase the activity of renin, indicating the absence of an inactive form of renin in rat kidneys, whereas pig renin was activated by this procedure. Pig renin has isoelectric points at pH 4.6, 4.8, 5.05 and 5.2, significantly lower than for rat renin. The isoenzymes from the two species had no antigenicity in common, as shown by crossed immunoelectrophoresis or rocket immunoelectrophoresis. The Michaelis constants for pig and rat renin were in the same range, 1x10-6M, when rat renin substrate was used. The relative content of rat isoenzyme with pI in the pH ranges 4.9-5.1, 5.1-5.3 and 5.3-5.5 was approx. 20, 27 and 53% respectively. Purified pig renin prepared in two different ways had isoenzymes with pI in the pH regions 4.5-4.7, 4.7-4.9, 4.9-5.05 and 5.05-5.20 in the approximate proportions 14, 24, 28 and 29%.

UR - http://www.scopus.com/inward/record.url?scp=0017065293&partnerID=8YFLogxK

U2 - 10.1042/bj1550317

DO - 10.1042/bj1550317

M3 - Journal article

C2 - 938482

AN - SCOPUS:0017065293

VL - 155

SP - 317

EP - 323

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -