Immunoglobulin structure: variation in amino acid sequence and length of human lambda light chains.

Science (New York, N.Y.) ·Vol. 157 ·No. 3792 ·1967-09-01 ·Pages 1050-3

Putnam FW, Shinoda T, Titani K, Wikler M

Abstract

Variation and conservation in the primary structure of human lambda light chains is revealed by complete amino acid sequence of three Bence Jones proteins. These proteins differ in amino acid sequence in from 38 to 48 positions; they are of unequal length in the amino-terminal half of the chain but have identical sequence in the last 105 amino acids.

MeSH Terms

Amino Acid Sequence Bence Jones Protein/analysis Biological Evolution Carboxypeptidases Chymotrypsin Humans In Vitro Techniques Leucyl Aminopeptidase Mutation Peptides/analysis gamma-Globulins/analysis

Chemicals

Peptides gamma-Globulins Bence Jones Protein Carboxypeptidases Leucyl Aminopeptidase Chymotrypsin

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Putnam F W

Shinoda T

Titani K

Wikler M

Article Info

Journal

Science (New York, N.Y.)

Abbr.

Science

ISSN

0036-8075

DOI

10.1126/science.157.3792.1050

Published

1967-09-01

Pages

1050-3

Language

English

Region

United States

NLM ID

0404511

Subset

External Links

PubMed source DOI: 10.1126/science.157.3792.1050 View journal details

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Immunoglobulin structure: variation in amino acid sequence and length of human lambda light chains.

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