N-terminal sequence heterogeneity of guinea pig anti-DNP kappa chains

J. A. Grant, M. E. Lamm, L. Hood

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The amino acids present at the first four N-terminal positions of light chains derived from guinea pig pooled normal immunoglobulins and a purified anti-DNP antibody were determined quantitatively. Light chains from both sources were heterogeneous, and the quantitative yields of predominant amino acids were similar. This indicates that the DNP determinant does not select for a single specificity region in the antibody light chains of guinea pigs. Qualitatively, the amino acids observed at each position were the same ones seen at the comparable positions of normal human light chains, suggesting the existence of guinea pig specificity region subclasses.

Original languageEnglish (US)
Pages (from-to)645-648
Number of pages4
JournalImmunochemistry
Volume6
Issue number5
StatePublished - Sep 1967

Fingerprint

Guinea Pigs
Light
Amino Acids
Immunoglobulins
Anti-Idiotypic Antibodies
Antibodies

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Grant, J. A., Lamm, M. E., & Hood, L. (1967). N-terminal sequence heterogeneity of guinea pig anti-DNP kappa chains. Immunochemistry, 6(5), 645-648.

N-terminal sequence heterogeneity of guinea pig anti-DNP kappa chains. / Grant, J. A.; Lamm, M. E.; Hood, L.

In: Immunochemistry, Vol. 6, No. 5, 09.1967, p. 645-648.

Research output: Contribution to journalArticle

Grant, JA, Lamm, ME & Hood, L 1967, 'N-terminal sequence heterogeneity of guinea pig anti-DNP kappa chains', Immunochemistry, vol. 6, no. 5, pp. 645-648.
Grant, J. A. ; Lamm, M. E. ; Hood, L. / N-terminal sequence heterogeneity of guinea pig anti-DNP kappa chains. In: Immunochemistry. 1967 ; Vol. 6, No. 5. pp. 645-648.
@article{f0bab1e3cda54aaba201621485981c54,
title = "N-terminal sequence heterogeneity of guinea pig anti-DNP kappa chains",
abstract = "The amino acids present at the first four N-terminal positions of light chains derived from guinea pig pooled normal immunoglobulins and a purified anti-DNP antibody were determined quantitatively. Light chains from both sources were heterogeneous, and the quantitative yields of predominant amino acids were similar. This indicates that the DNP determinant does not select for a single specificity region in the antibody light chains of guinea pigs. Qualitatively, the amino acids observed at each position were the same ones seen at the comparable positions of normal human light chains, suggesting the existence of guinea pig specificity region subclasses.",
author = "Grant, {J. A.} and Lamm, {M. E.} and L. Hood",
year = "1967",
month = "9",
language = "English (US)",
volume = "6",
pages = "645--648",
journal = "Molecular Immunology",
issn = "0161-5890",
publisher = "Elsevier Limited",
number = "5",

}

TY - JOUR

T1 - N-terminal sequence heterogeneity of guinea pig anti-DNP kappa chains

AU - Grant, J. A.

AU - Lamm, M. E.

AU - Hood, L.

PY - 1967/9

Y1 - 1967/9

N2 - The amino acids present at the first four N-terminal positions of light chains derived from guinea pig pooled normal immunoglobulins and a purified anti-DNP antibody were determined quantitatively. Light chains from both sources were heterogeneous, and the quantitative yields of predominant amino acids were similar. This indicates that the DNP determinant does not select for a single specificity region in the antibody light chains of guinea pigs. Qualitatively, the amino acids observed at each position were the same ones seen at the comparable positions of normal human light chains, suggesting the existence of guinea pig specificity region subclasses.

AB - The amino acids present at the first four N-terminal positions of light chains derived from guinea pig pooled normal immunoglobulins and a purified anti-DNP antibody were determined quantitatively. Light chains from both sources were heterogeneous, and the quantitative yields of predominant amino acids were similar. This indicates that the DNP determinant does not select for a single specificity region in the antibody light chains of guinea pigs. Qualitatively, the amino acids observed at each position were the same ones seen at the comparable positions of normal human light chains, suggesting the existence of guinea pig specificity region subclasses.

UR - http://www.scopus.com/inward/record.url?scp=0014579257&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0014579257&partnerID=8YFLogxK

M3 - Article

VL - 6

SP - 645

EP - 648

JO - Molecular Immunology

JF - Molecular Immunology

SN - 0161-5890

IS - 5

ER -