Purification of rat renal renin from crude kidney extracts by diaminohexamethylene-Sepharose chromatography
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Purification of rat renal renin from crude kidney extracts by diaminohexamethylene-Sepharose chromatography. / Lauritzen, Edgar; Lauritzen, Martin; Rubin, Inger.
In: Topics in Catalysis, Vol. 96, No. 2, 01.01.1980, p. 907-914.Research output: Contribution to journal › Journal article › Research › peer-review
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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
VL - 96
SP - 907
EP - 914
JO - Topics in Catalysis
JF - Topics in Catalysis
SN - 1022-5528
IS - 2
ER -
ID: 214392629