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Title: Radioiodination of chicken luteinizing hormone without affecting receptor binding potency

Abstract

By improving the currently used lactoperoxidase method, we were able to obtain radioiodinated chicken luteinizing hormone (LH) that shows high specific binding and low nonspecific binding to a crude plasma membrane fraction of testicular cells of the domestic fowl and the Japanese quail, and to the ovarian granulosa cells of the Japanese quail. The change we made from the original method consisted of (1) using chicken LH for radioiodination that was not only highly purified but also retained a high receptor binding potency; (2) controlling the level of incorporation of radioiodine into chicken LH molecules by employing a short reaction time and low temperature; and (3) fractionating radioiodinated chicken LH further by gel filtration using high-performance liquid chromatography. Specific radioactivity of the final {sup 125}I-labeled chicken LH preparation was 14 microCi/micrograms. When specific binding was 12-16%, nonspecific binding was as low as 2-4% in the gonadal receptors. {sup 125}I-Labeled chicken LH was displaced by chicken LH and ovine LH but not by chicken follicle-stimulating hormone. The equilibrium association constant of quail testicular receptor was 3.6 x 10(9) M-1. We concluded that chicken LH radioiodinated by the present method is useful for studies of avian LH receptors.

Authors:
;  [1]
  1. Waseda Univ., Tokyo (Japan)
Publication Date:
OSTI Identifier:
7138016
Resource Type:
Journal Article
Journal Name:
Biology of Reproduction; (USA)
Additional Journal Information:
Journal Volume: 41:6; Journal ID: ISSN 0006-3363
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; LH; RECEPTORS; BIOCHEMICAL REACTION KINETICS; BIRDS; CELL MEMBRANES; CHICKENS; FRACTIONATION; FSH; IODINATION; IODINE 125; LIQUID COLUMN CHROMATOGRAPHY; RADIOIMMUNOASSAY; ANIMALS; BETA DECAY RADIOISOTOPES; BIOASSAY; CELL CONSTITUENTS; CHEMICAL REACTIONS; CHROMATOGRAPHY; DAYS LIVING RADIOISOTOPES; DIAGNOSTIC TECHNIQUES; ELECTRON CAPTURE RADIOISOTOPES; FOWL; GONADOTROPINS; HALOGENATION; HORMONES; IMMUNOASSAY; IMMUNOLOGY; INTERMEDIATE MASS NUCLEI; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; KINETICS; MEMBRANE PROTEINS; MEMBRANES; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; PEPTIDE HORMONES; PITUITARY HORMONES; PROTEINS; RADIOASSAY; RADIOIMMUNODETECTION; RADIOIMMUNOLOGY; RADIOISOTOPES; REACTION KINETICS; SEPARATION PROCESSES; TRACER TECHNIQUES; VERTEBRATES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Kikuchi, M, and Ishii, S. Radioiodination of chicken luteinizing hormone without affecting receptor binding potency. United States: N. p., 1989. Web. doi:10.1095/biolreprod41.6.1047.
Kikuchi, M, & Ishii, S. Radioiodination of chicken luteinizing hormone without affecting receptor binding potency. United States. https://doi.org/10.1095/biolreprod41.6.1047
Kikuchi, M, and Ishii, S. 1989. "Radioiodination of chicken luteinizing hormone without affecting receptor binding potency". United States. https://doi.org/10.1095/biolreprod41.6.1047.
@article{osti_7138016,
title = {Radioiodination of chicken luteinizing hormone without affecting receptor binding potency},
author = {Kikuchi, M and Ishii, S},
abstractNote = {By improving the currently used lactoperoxidase method, we were able to obtain radioiodinated chicken luteinizing hormone (LH) that shows high specific binding and low nonspecific binding to a crude plasma membrane fraction of testicular cells of the domestic fowl and the Japanese quail, and to the ovarian granulosa cells of the Japanese quail. The change we made from the original method consisted of (1) using chicken LH for radioiodination that was not only highly purified but also retained a high receptor binding potency; (2) controlling the level of incorporation of radioiodine into chicken LH molecules by employing a short reaction time and low temperature; and (3) fractionating radioiodinated chicken LH further by gel filtration using high-performance liquid chromatography. Specific radioactivity of the final {sup 125}I-labeled chicken LH preparation was 14 microCi/micrograms. When specific binding was 12-16%, nonspecific binding was as low as 2-4% in the gonadal receptors. {sup 125}I-Labeled chicken LH was displaced by chicken LH and ovine LH but not by chicken follicle-stimulating hormone. The equilibrium association constant of quail testicular receptor was 3.6 x 10(9) M-1. We concluded that chicken LH radioiodinated by the present method is useful for studies of avian LH receptors.},
doi = {10.1095/biolreprod41.6.1047},
url = {https://www.osti.gov/biblio/7138016}, journal = {Biology of Reproduction; (USA)},
issn = {0006-3363},
number = ,
volume = 41:6,
place = {United States},
year = {Fri Dec 01 00:00:00 EST 1989},
month = {Fri Dec 01 00:00:00 EST 1989}
}