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A new type of temperature-dependent serum M protein: a case of IgG-lambda type multiple myeloma
Mayumi Imoto1, Hyogo Sinohara, Ikunosuke Sakurabayashi
1Department of Central Clinical Laboratory, Kinki University Hospital 377-2, Ohnohigashi, Osakasayama, 589-8511, Osaka, Japan. maimoto@zmail.plala.or.jp
Background:
We report a rare case of temperature-dependent serum M protein (thermoprotein), monoclonal IgG(1)-lambda protein isolated from 90-year-old female with advanced multiple myeloma.
Methods:
M protein was identified in the blood plasma of the patient by immunoelectrophoresis (IEP). To evaluate the types of bonds, the properties of the protein after reduction and chemical treatment were examined.
Results:
This protein was irreversibly precipitated at or above room temperature when exposed in the air. This protein was redissolved by 30 mmol/l dithiothreitol, 4 mol/l urea, or 8 mmol/l EDTA.
Conclusions:
Unlike other immunoglobulins reported to date, this data suggests that hydrogen, disulfide, and ionic bonds are involved in the temperature-dependent precipitation of this M protein.
Insights
A rare temperature-dependent M protein (thermoprotein), a monoclonal IgG(1)-lambda, was found in a multiple myeloma patient. This unique protein precipitates at room temperature, suggesting novel bonding interactions.
Area of Science:
- Biochemistry
- Immunology
- Hematology
Background:
- Presents a rare case of temperature-dependent serum M protein (thermoprotein) in a 90-year-old female with advanced multiple myeloma.
- The M protein was identified as a monoclonal IgG(1)-lambda immunoglobulin.
Observation:
- The M protein exhibited irreversible precipitation at or above room temperature when exposed to air.
- This thermoprotein could be redissolved using dithiothreitol, urea, or EDTA.
Findings:
- The study investigated the properties of the M protein after reduction and chemical treatment.
- Analysis suggests the involvement of hydrogen, disulfide, and ionic bonds in the temperature-dependent precipitation of this M protein.
Implications:
- This finding offers new insights into the structural characteristics of immunoglobulins.
- Understanding the unique bonding in thermoproteins could inform future therapeutic strategies for multiple myeloma and related disorders.