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M and the
M Monomer Derived by Reduction and Alkylation of 19 S
M1From the Mayo Clinic and Mayo Foundation, Sections of Medicine and Microbiology, Rochester, Minnesota, and the Department of Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York
Abstract
A naturally occurring low molecular weight
M protein (
MN) was isolated from the serum of a patient with type I dysgammaglobulinemia by preparative electrophoresis and gel filtration. This protein was compared to the macroglobulin (
M19) isolated from the patient's serum and to the
M subunit (
MS) prepared by reduction and alkylation of
M19. The results indicate that
MN and
MS are similar in size and have the same antigenic determinants. These observations support the concept that the
MN is a naturally occurring subunit of
M19 and is very similar to
MS,
M19,
MN and
MS were also prepared from the patient's serum after tetanus immunization and were found to bind radiolabeled tetanus toxoid. Most, but not all, controls did not show nonspecific binding of tetanus toxoid. These results suggest but do not conclusively establish the capacity of these
M proteins to bind antigen specifically.
Footnotes
1 A preliminary report of this work was presented at the meeting of the American Academy of Allergy, Palm Springs, California (1), February 18 to 22, 1967. This investigation was supported in part by Research Grants AI-7187, FP-44 and AM-2443 from the National Institutes of Health, Public Health Service.
2 Mayo Clinic and Mayo Foundation.
3 University of Rochester School of Medicine and Dentistry.
Present address: Department of Medicine, University of Western Ontario, London, Ontario, Canada.
This article has been cited by other articles:
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R. C. Griggs, W. Strober, and D. E. McFarlin Recurrent Encephalopathy: Associated With Low Molecular Weight {gamma}M in the Serum and Cerebrospinal Fluid Arch Neurol, September 1, 1969; 21(3): 303 - 314. [Abstract] [PDF] |
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