当前位置： SCI文献检索 > PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA期刊下所有文献 > Amino-acid sequences of light chains of a rabbit anti-p-azobenzoate antibody.

Amino-acid sequences of light chains of a rabbit anti-p-azobenzoate antibody.

Abstract：

:Half-cystine peptic peptides representing the intrachain disulfide bonds of the light chain from an apparently homogeneous rabbit anti-p-azobenzoate antibody were isolated in good yields after reduction and alkylation with [(14)C]iodoacetate, and their sequences were determined. The sequence of the first 21 amino-terminal residues was also determined. The good yields of these peptides, the fact that no variants of any of them were found, and the cleanness of the amino-terminal sequence determination confirm the high degree of homogeneity of this light-chain preparation. Previous evidence for the homogeneity of the light chain includes the appearance of only a single band upon analysis by disc electrophoresis, a relatively unique amino-acid composition, and a simple tryptic peptide map. The whole antibody shows a homogeneity of the hapten-binding constant. The antigen used in the present work is complex, since the attached hapten groups are in a large variety of environments, particularly since the carrier is a heterogeneous mixture of globulins. The very limited heterogeneity of the antibodies found in this case would appear to depend on the stimulation of only a few of the cells capable of producing antibody against a given hapten, rather than on a structural identity of the environment around each individual hapten group that is located on the antigen molecule.

journal_name

Proc Natl Acad Sci U S A

journal_title

Proceedings of the National Academy of Sciences of the United States of America

authors

Appella E,Chersi A,Roholt OA,Pressman D

doi

10.1073/pnas.68.10.2569

subject

Has Abstract

pub_date

1971-10-01 00:00:00

pages

2569-73

issue

10

eissn

0027-8424

issn

1091-6490

journal_volume

68

pub_type

杂志文章

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