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Science 15 October 1965:
Vol. 150. no. 3694, pp. 361 - 363
DOI: 10.1126/science.150.3694.361
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Articles

Macroglobulin-Producing Plasma-Cell Tumor in Mice: Identification of a New Light Chain

K. R. Mcintimif 1, R. M. Asofsky 1, M. Potter 1, and E. L. Kuff 1

1 National Cancer Institute and National Institute of Allergy and Infectious, Disease. Bethesda, Maryland 20014

A transplantable plasmacell tumor in mice produces both a ggrM-macroglobulin serum protein with a sedimentation coefficient of 17S and a kappa-type urinary protein. The reduced and alkylated macroglobulin, when examined by electrophoresis in acid-urea polyacrylamide gel, had a fast component which migrated in the same position as the urinary protein and also a slow component. These two components, as shown by exclusion chromatography, represent the light and heavy polypeptide chains of the ggrM-macroglobulin. The aforementioned macroglobulin was antigenically related to that in normal mouse serum.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Malfunction of Cerebral Microcirculation in Macroglobulinemic Mice: Relationship to Increased Blood Viscosity.
W. I. Rosenblum and R. M. Asofsky (1968)
Arch Neurol 18, 151-159
   Abstract »    PDF »
Two Types Of Lambda Polypeptide Chains In Human Immunoglobulins.
D. Ein and J. L. Fahey (1967)
Science 156, 947-948
   Abstract »    PDF »
The Structure of Immunoglobulin Light Chains.
E. Appella and R. N. Perham (1967)
Cold Spring Harb Symp Quant Biol 32, 37-44
   Abstract »    PDF »
Light Chains of Mouse Myeloma Proteins: Partial Amino Acid Sequence.
R. Perham, E. Appella, and M. Potter (1966)
Science 154, 391-393
   Abstract »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)