Studies of the egg proteins of tropical lizards: purification and partial characterization of yolk proteins of Anolis pulchellus.
An easy biochemical procedure for the isolation of lizard lipoprotein is presented as well as the partial characterization of several egg proteins from tropical lizards. In Anolis pulchellus the egg content which is very yolky is homogeneously distributed throughout the egg with no apparent presence of an egg-white. Nevertheless, after resuspension in 0.02 M glycine (pH 7.2), a yolk pellet and a fraction with soluble proteins were separated by low-speed centrifugation. By chromatography in Sephadex G-100, the major egg yolk protein (S-1) was highly purified. This protein was characterized as a glyco-lipo-phosphoprotein with a mol wt of 110,000-120,000 as shown by SDS PAGE. By DEAE cellulose chromatography two acidic proteins (D-5; D-6) were purified (Mr = 62,000-66,000), which do not seem to be components of the yolk granules. Protein D-5 was shown to be a Fe2+-binding protein. By immunochemistry, the liver was found to be the site of synthesis of S-1 and D-5; both proteins are female specific. It is also demonstrated that S-1 shares several chemical and structural properties with the lipovitellins from other oviparous animals.
D000818:Animals; D000906:Antibodies / Q000276:immunology; D000918:Antibody Specificity; D002850:Chromatography, Gel / Q000379:methods; D004527:Egg Proteins / Q000276:immunology / Q000302:isolation & purification* / Q000378:metabolism* / Q000502:physiology; D004530:Egg Yolk; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007120:Immunochemistry; D005779:Immunodiffusion; D008116:Lizards / Q000378:metabolism*; D008970:Molecular Weight; D012098:Reproduction
D000906:Antibodies; D004527:Egg Proteins