Purification of rat renal renin from crude kidney extracts by diaminohexamethylene-Sepharose chromatography

TY - JOUR

T1 - Purification of rat renal renin from crude kidney extracts by diaminohexamethylene-Sepharose chromatography

AU - Lauritzen, Edgar

AU - Lauritzen, Martin

AU - Rubin, Inger

PY - 1980/1/1

Y1 - 1980/1/1

N2 - Renin from rat kidney extracts was adsorbed to diaminohexamethylene-sepharose columns at extremely low ionic strength and neutral pH. Renin was retarded while the column was developed in 1 mM sodiumpyrophosphate and extraneous proteins were removed. Elution of renin was performed using a linear gradient of sodiumpyrophosphate, 1 – 17 mM at pH 6.8. Renin was purified in a yield up to approx. 60 per cent of the applied activity and a purification factor between 5 – 122 depending on the specific activity of the applied sample. The specific activity after this single chromatography of crude rat kidney homogenate on diaminohexamethylene-sepharose showed a median of 11.3 Goldblatt units per mg protein in a range of 5.3 – 42.0 Goldblatt units per mg protein. The renin binding capacity of the column was 1 Goldblatt unit per ml wet gel. The purified renin was subjected to G-100 Sephadex chromatography demonstrating two molecular weight forms of 44000 and 50000 dalton. Polyacrylamide gel electrophoresis demonstrated three separate fractions of renin.

AB - Renin from rat kidney extracts was adsorbed to diaminohexamethylene-sepharose columns at extremely low ionic strength and neutral pH. Renin was retarded while the column was developed in 1 mM sodiumpyrophosphate and extraneous proteins were removed. Elution of renin was performed using a linear gradient of sodiumpyrophosphate, 1 – 17 mM at pH 6.8. Renin was purified in a yield up to approx. 60 per cent of the applied activity and a purification factor between 5 – 122 depending on the specific activity of the applied sample. The specific activity after this single chromatography of crude rat kidney homogenate on diaminohexamethylene-sepharose showed a median of 11.3 Goldblatt units per mg protein in a range of 5.3 – 42.0 Goldblatt units per mg protein. The renin binding capacity of the column was 1 Goldblatt unit per ml wet gel. The purified renin was subjected to G-100 Sephadex chromatography demonstrating two molecular weight forms of 44000 and 50000 dalton. Polyacrylamide gel electrophoresis demonstrated three separate fractions of renin.

UR - http://www.scopus.com/inward/record.url?scp=0019202680&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(80)91441-2

DO - 10.1016/0006-291X(80)91441-2

M3 - Journal article

C2 - 7000074

AN - SCOPUS:0019202680

SN - 1022-5528

VL - 96

SP - 907

EP - 914

JO - Topics in Catalysis

JF - Topics in Catalysis

IS - 2

ER -