{'fraction_non_alphanumeric': 0.032230703986429174, 'fraction_numerical': 0.0016963528413910093, 'mean_word_length': 5.742857142857143, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Simple and Sensitive Detection of Vitellogenin Receptor(s) in Sakhalin Taimen (Hucho perryi)

Oocyte membranes from vitellogenic ovarian follicles in Sakhalin taimen (Hucho perryi) were solubilized using a detergent, n-octyl-,8-D-glucopylanoside. Taimen vitellogenin receptor(s) (VGR) in the extracts was visualized by enhanced chemical luminescence (ECL)-ligand blotting using biotinylated vitellogenin as a probe. The ovarian membranes revealed five receptor proteins in the ligand blotting under non-reducing condition. When the excess volume of non-biotinylated vitellogenin was added, or biotinylated bovine serum albumin was used as another probe, the receptor proteins could not be detected, indicating that the receptor proteins were specific for Vg. To obtain an information for the receptor binding site in V g molecule, displacement of biotinylated V g from ovarian membrane extracts by vitellogenin-derived competitive ligands was conducted. Lipovitellin could displace the labeled vitellogenin as well as vitellogenin, while ,8' -component and phosvitin showed less replacement, indicating that the major receptor-binding site is lipovitellin domain in V g molecule.