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Related Experiment Video

Updated: Jul 16, 2026

Extra Cellular Matrix-Based and Extra Cellular Matrix-Free Generation of Murine Testicular Organoids

Extra Cellular Matrix-Based and Extra Cellular Matrix-Free Generation of Murine Testicular Organoids

Published on: October 7, 2020

Three-dimensional structures of gonadotropins

J W Lustbader¹, S Pollak, L Lobel

¹Columbia University, College of Physicians and Surgeons, New York 10032, USA.

Molecular and Cellular Endocrinology

|December 20, 1996

Summary

Researchers developed a novel isotope-labeling medium for Chinese hamster ovary cells, enabling structural determination of biologically active human chorionic gonadotropin (hCG) and other glycoproteins.

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Area of Science:

Biochemistry
Structural Biology
Glycoprotein Research

Background:

Secreted proteins, including human chorionic gonadotropin (hCG), are often glycosylated, posing challenges for structural determination via crystallography due to carbohydrate heterogeneity.
Chemical deglycosylation (e.g., HF treatment) yields non-biologically active hCG with altered subunit interactions, necessitating methods to study the native, active hormone.

Purpose of the Study:

To develop a method for determining the structure of biologically active, glycosylated hCG and its subunits in solution.
To overcome limitations of crystallographic studies for heterogeneous glycoproteins.

Main Methods:

Development of a universal, nonradioactive isotope-labeling medium enriched in carbon-13 (13C) and nitrogen-15 (15N).
Expression of uniformly labeled hCG in Chinese hamster ovary (CHO) cells.
Biochemical, immunochemical, and biological activity comparisons of recombinant hCG with urinary hCG.
Mass spectrometry and preliminary NMR structural analysis of labeled hCG.

Main Results:

Uniform isotope labeling (over 90% incorporation) of recombinant hCG and its subunits was achieved using the developed medium.
Isotopically labeled hCG and its subunits were biochemically, immunochemically, and biologically indistinguishable from native urinary hCG.
Preliminary NMR data confirmed uniform labeling sufficient for structural studies.

Conclusions:

The developed 13C and 15N-enriched labeling medium is a technological advancement enabling structural determination of biologically active glycoproteins, including hCG.
This method facilitates the study of other challenging glycoproteins unsuitable for crystallographic analysis.