Studies on a kallikrein-kinin system in plasma of patients with acute pancreatitis: the preparation and characterization of a kallikrein-like enzyme in patient's plasma.
In a previous paper, the authors reported that the kallikrein-like activity was eluted in alpha 2-macroglobulin fractions when patient's plasma was fractionated with Sephadex G-200 gel filtration. In order to clarify the characteristics of the kallikrein-like enzyme, enzyme isolation methods were investigated. Success was attained by the addition of 1 % sodium-dodecyl-sulfate to alpha 2-macroglobulin fractions followed by G-200 chromatography. It was also confirmed that alpha 2-macroglobulin from which the enzyme was removed regained antiplasmin activity, and that some proteases other than the kallikrein-like enzyme were also bound to alpha 2-macroglobulin. The kallikrein-like enzyme isolated by sodium-dodecyl-sulfate-treatment was examined in respect of its molecular weight and its ability to be adsorbed on DEAE-cellulose and was found to possess a molecular weight approximating that of ovalbumin or human pancreatic kallikrein and a binding affinity for DEAE-cellulose. From these results, the authors speculate that during attacks of acute pancreatitis, the pancreas liberates kallikrein into the blood.
D000208:Acute Disease; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D005341:Fibrinolysin / Q000378:metabolism; D006801:Humans; D007610:Kallikreins / Q000097:blood / Q000302:isolation & purification*; D010195:Pancreatitis / Q000201:enzymology*; D014462:Ultrafiltration; D000511:alpha-Macroglobulins / Q000032:analysis
D000511:alpha-Macroglobulins; D007610:Kallikreins; D005341:Fibrinolysin