The endogenous lectins of the chick blastoderm are present in association with an apolipoprotein in distinct organelles and in the extracellular matrix.

Affinity purified preparations of the galactose-binding lectin from gastrulating chick blastoderms consist of three main polypeptides. Two of these have been identified as the 14 kD and 16 kD galactose-binding lectins. A third one migrates in SDS-PAGE gels with a relative molecular weight of 6,500±500 and has been identified as an apolipoprotein (Apo) of plasma very low density lipoproteins, Apo-VLDL-II. We have studied the localization of these polypeptides using immunofluorescence and ultrastructural immunocytochemistry with peroxidase and protein-A gold. The 14 kD lectin occurs in the intracellular yolk where it is mainly present within the electron lucent component. The 16 kD is also present in the intracellular yolk platelets, but tends to predominate in the electron-dense component. In addition, the 16 kD lectin is also present in pleiomorphic yolk-associated organelles and in the extracellular matrix. Apo-VLDL-II is also localized in the electron-lucent component of the yolk platelet and in the extracellular matrix. Our results suggest that the lectin(s) are associated with Apo-VLDL-II in the yolk platelet, and may subsequently become externalized.