Studies on Acute Phase Proteins of Rat Serum. IV. Pathway of Secretion of Albumin and α1-Acid Glycoprotein from Liver

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Abstract
Normal rats and those suffering from inflammation for 12 h were given pulse injections of L-leucine-3H and D-glucosamine-14C and were killed at 3–60 min thereafter. Rough and smooth microsome fractions and a Golgi-enriched fraction were prepared from liver and the fractions were extracted with the non-ionic detergent Lubrol-W. Albumin and acute phase α1-acid glycoprotein were isolated from the extracts by application of a quantitative precipitin technique employing antisera to albumin and α1-acid glycoprotein, and specific radioactivities were determined. The results indicated that the pathway of secretion of albumin and α1-acid glycoprotein was rough endoplasmic reticulum → smooth endoplasmic reticulum → Golgi complex → blood. Although there was little difference in the pathway or rate of secretion of the proteins under study in normal and experimental animals, there was an increase in specific radioactivities of labelled leucine and glucosamine associated with α1-acid glycoprotein when isolated from subcellular fractions from livers from experimental animals.

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