# CHEMISTRY AND BIOLOGY OF HUMAN AND OTHER GONADOTROPINS

> **NIH NIH R01** · STATE UNIVERSITY OF NEW YORK AT BUFFALO · 1994 · $192,804

## Abstract

The proposed studies relating to the structure and function
relationships in human choriogonadotropin (hCG) and its receptor are a
continuation of our ongoing studies.  HCG and its subunits and the rat
lutropin receptor have been expressed in an heterologous eukaryotic
expression system, baculovirus-insect cell system.  The hormone and its
subunits were expressed in a high efficiency and could be purified by
immunoaffinity chromatography.  Since the recombinant hormones are
similar to the native hormone and its subunits in immunological and
biological properties, they can replace the native urinary hormones in
all immunodiagnostic applications.  More importantly, it has been
possible to substitute selenomethionine for methionine in hCG.  The
recombinant selenomethionyl hCG has considerable potential in the
determination of its three dimensional structure.  The recombinant
LH/hCG receptor expressed in baculovirus system occurs predominantly as
a dimer.  The specific aims of the present studies are twofold. I.
Studies on the structure and function relationships of gonadotropins
will include the preparation and characterization of: (1) Recombinant
selenomethionyl hCG on a large scale and to attempt to obtain x-ray
diffraction grade crystals for three dimensional structural analysis.
(2) Recombinant unglycosylated hCG and its subunits to resolve the
question of the carbohydrate role in the function of hCG and
selenomethionyl unglycosylated hCG. (3) The polypeptide and carbohydrate
chains of recombinant hCG and its subunits. (4) Recombinant hCG,
hCGalpha and hCGbeta on a large scale for further evaluation of their in
vivo biological properties. (5) Carbohydrate mutants of hCGalpha and
hCGbeta in baculovirus expression system to evaluate the contribution of
individual N-linked carbohydrates to the function of hCG. II. Studies on
the structure and function of rat LH/hCG receptor will include the
preparation and characterization of: (1) Recombinant rat LH/hCG
receptor. (2)Recombinant 1-294 amino acid residue extracellular
polypeptide and its selenomethionyl analog.  (3) Various deletion
mutants of LH/hCG receptor in insect cells in order to delineate the
ligand binding domain of the receptor and (4) Delineation of the hormone
and Gs binding sites of the LH/hCG receptor and the possible involvement
of extracellular and cytoplasmic loops in the ligand or Gs binding
respectively.  (5) Homologous reconstitution of LH receptor with GTP
binding protein (Gs) and with Gs and adenylate cyclase or phospholipase
C from rat ovarian membranes in liposomes to study the role of
carbohydrate in the hormone and the receptor in the mechanism of signal
transduction.  All of the above studies should enhance our understanding
of the regulation of human fertility and thus facilitate the development
of safer methods of contraception.

## Key facts

- **NIH application ID:** 2196629
- **Project number:** 5R01HD008766-28
- **Recipient organization:** STATE UNIVERSITY OF NEW YORK AT BUFFALO
- **SAM.gov UEI:** LMCJKRFW5R81
- **Principal Investigator:** OM P BAHL
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1994
- **Award amount:** $192,804
- **Award type:** 5
- **Project period:** 1977-12-01 → 1997-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/2196629

## Citation

> US National Institutes of Health, RePORTER application 2196629, CHEMISTRY AND BIOLOGY OF HUMAN AND OTHER GONADOTROPINS (5R01HD008766-28). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/2196629. Licensed CC0.

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