The estimation and comparison of molecular weight of angiotensin I converting enzyme by sodium dodecyl sulfate-polyacrylamide gel eletrophoresis.
The angiotensin I converting enzyme from rat lung was observed to be a glycoprotein containing 8.3% carbohydrate and consisting of a single polypeptide chain with an estimated molecular weight of 139 000 as determined by sodium dodecylsulfate-polyacrylamide gel electrophoresis and 150 000 by sucrose density gradient sedimentation analysis. A comparison of the mobility of angiotensin I converting enzyme from rat lung, rabbit lung, and two hog lung sources on sodium dodecyl sulfate-polyacrylamide gels indicates that all four enzymes have very similar molecular weights and subunit structures. Some previously reported molecular weight discrepancies appear to be due to anomalous behavior of the enzyme of gel filtration.
D000818:Animals; D002499:Centrifugation, Density Gradient; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D008168:Lung / Q000201:enzymology; D008970:Molecular Weight; D009928:Organ Specificity; D007703:Peptidyl-Dipeptidase A; D051381:Rats; D012967:Sodium Dodecyl Sulfate; D013045:Species Specificity
D012967:Sodium Dodecyl Sulfate; D007703:Peptidyl-Dipeptidase A