Abstract
Abstract Previous claims that could be detected in subcellular particles of rat liver by coagulation assays have been shown to be based on the artifactual conversion of residual in the reagents to thrombin by lysosomal cathepsin C. The heavy microsome fraction, rich in lysosomes, and prothrombin did not carry out general protein synthesis under the conditions of apparent biosynthesis. The reduced apparent observed in liver microsomes from vitamin K-deficient rats is due to an alteration in the integrity of lysosomes in this deficiency disease. Application of a radiommunoassay for to the detection of in rat liver microsomes before and after incubation showed that the actual content ranged, respectively, from 2 to 10 ng per mg of microsomal protein. The highest amount of detected is only one-tenth of that required to give a reliable coagulation assay.
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