Electrophoretic heterogeneity of the polypeptide chains of human G-myeloma proteins.

Science (New York, N.Y.) ·Vol. 152 ·No. 3729 ·1966-06-17 ·Pages 1628-30

Terry WD, Small PA, Reisfeld RA

Abstract

The light and heavy polypeptide chains derived from human Gmyeloma proteins are electrophoretically heterogeneous as judged by disc electrophoresis of the polypeptide chains in urea-acrylamide gels. Individual myeloma proteins contained as many as eight light-chain and nine heavy-chain components.

MeSH Terms

Blood Protein Electrophoresis Humans In Vitro Techniques Multiple Myeloma Ultracentrifugation gamma-Globulins

Chemicals

gamma-Globulins

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Terry W D

Small P A

Reisfeld R A

Article Info

Journal

Science (New York, N.Y.)

Abbr.

Science

ISSN

0036-8075

DOI

10.1126/science.152.3729.1628

Published

1966-06-17

Pages

1628-30

Language

English

Region

United States

NLM ID

0404511

Subset

External Links

PubMed source DOI: 10.1126/science.152.3729.1628 View journal details

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Electrophoretic heterogeneity of the polypeptide chains of human G-myeloma proteins.

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