Purification and characterization of beta-galactoside binding lectin from frog (Rana catesbeiana) eggs.
A beta-galactoside-binding lectin, a homodimer composed of 14kDa subunits, was purified from unfertilized eggs of the frog Rana catesbeiana by asialofetuin-Sepharose 4B affinity column chromatography. The lectin was solubilized from eggs by addition of neither haptenic sugar nor detergent and showed a unique characteristic that it requires neither Ca++ nor SH-reagent for its hemagglutination activity. However, the partial amino acid sequence indicated that the lectin belongs to a family of soluble 14kDa beta-galactoside-binding lectins (14K-lectin) widely distributed in vertebrates and classified as S type lectins. These results indicate that a 14K-lectin is present as the free form in unfertilized frog eggs, presenting the first structural evidence for the presence of a soluble 14K-lectin in the amphibian eggs.
Ozeki
Y
Y
Division of Biomedical Polymer Science, School of Medicine, Fujita Health University, Aichi, Japan.
Matsui
T
T
Nitta
K
K
Kawauchi
H
H
Takayanagi
Y
Y
Titani
K
K
D000595:Amino Acid Sequence; D000818:Animals; D002241:Carbohydrates; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D005697:Galactosides / Q000378:metabolism; D037161:Galectins; D006384:Hemagglutination; D006388:Hemagglutinins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010063:Ovum / Q000502:physiology*; D010446:Peptide Fragments / Q000302:isolation & purification; D011892:Rana catesbeiana; D012689:Sequence Homology, Nucleic Acid
D002241:Carbohydrates; D005697:Galactosides; D037161:Galectins; D006388:Hemagglutinins; D010446:Peptide Fragments