# STUDIES OF HUMAN MONOCLONAL IGG CRYOGLOBULINS

> **NIH NIH R01** · UNIVERSITY OF ROCHESTER · 1987 · $130,007

## Abstract

Primary idiopathic IgG cryoglobulinemia is a disease whose clinical signs
are directly related to the presence of a circulating monoclonal IgG
cryoglobulin.  These proteins have the ability to self-associate in vivo
and in vitro and can thus aggregate or polymerize in a
concentration-dependent manner at temperatures of 37 C or less.  When the
cryoglobulin spontaneously appears and disappears, it possibly represents a
"normal" antibody, but with an unusual physical property.  Other
cryoglobulins may be formed as a paraprotein during a lymphoproliferative
or plasma cell dyscrasia.  Any cryoglobulin is presumed to contain diverse
primary structural mutations related to its ability to precipitate in the
cold.  These investigations will study the biophysical process of the
intermolecular self-associations and the primary structural properties of
the IgG cryoglobulins.

The intermolecular association process and possible temperature-induced
intramolecular conformational changes which cause cryoprecipitation will be
studied by three techniques:  circular dichroism spectroscopy, laser Raman
spectroscopy and the analytical ultracentrifuge.  Example of the three
morphologic types of IgG cryos so far defined, i.e., amorphous, gelatinous
and crystalline, will be studied.  The primary structure of these proteins
will be studied by primary amino acid sequence analysis of representative
cryoproteins:  specifically, those whose conformational properties have
been determined, and that subset which has cross-reactive idiotype like
determinants.  While the hypothesis is that mutations of primary structure
such as insertions or deletions will be noted at genomic splice points, the
entire V- region and junctional region structure will nevertheless be
determined.  It is felt that primary structural mutations may be present in
numerous regions of the molecules.  Finally, in order to demonstrate that
mutations found are specific, a non-cryoprecipitable IgG or matched heavy
chain subclass or light chain variable and constant region type will be
isolated from the same patient's serum and their primary structure defined.

## Key facts

- **NIH application ID:** 3129018
- **Project number:** 5R01AI019658-04
- **Recipient organization:** UNIVERSITY OF ROCHESTER
- **SAM.gov UEI:** F27KDXZMF9Y8
- **Principal Investigator:** George N. ABRAHAM
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $130,007
- **Award type:** 5
- **Project period:** 1984-04-01 → 1989-03-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3129018

## Citation

> US National Institutes of Health, RePORTER application 3129018, STUDIES OF HUMAN MONOCLONAL IGG CRYOGLOBULINS (5R01AI019658-04). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3129018. Licensed CC0.

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