Purification and Characterization Of a Thyroglobulin Reactive Phytoprecipitin From Pisum sativum

Abstract
By means of paper curtain electrophoresis and polyacrylaaide gel filtration, it has been possible to isolate the thyroglobulin-reactive phytoprecipitin from pea (Pisum sativum; American pea; Russian pea) extract. An of 4.0 Svedbergs and a of 5.7×10−7 cm2/sec were found from analytical ultracentrifuge experiments and a specific volume of 0.61 was determined by pycnometry. These data yield a molecular weight of 43,000 for the phytoprecipitin and, postulating an oblong ellipsoid shape, an asymmetry factor of 12. Its electro-phoretic mobility corresponds with that of globulin. It could be shown that the phytoprecipitin attaches to the carbohydrate part of the thyroglobulin.

This publication has 2 references indexed in Scilit: