scholarly journals The Amino Acid Sequence of the N-Terminal 84 Residues of a Human Heavy Chain of Immunoglobulin G (Daw)

1967 ◽  
Vol 104 (2) ◽  
pp. 30C-33C ◽  
Author(s):  
E. M. Press
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Immunoglobulin G

scholarly journals Sequence studies of the Fd section of the heavy chain of rabbit immunoglobulin G

1970 ◽  
Vol 116 (2) ◽  
pp. 249-259 ◽  
Author(s):  
R. G. Fruchter ◽  
S. A. Jackson ◽  
L. E. Mole ◽  
R. R. Porter
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Partial Amino Acid Sequence ◽  
Limited Region ◽  
Heavy Chains ◽  
Total Sequence ◽  
Continuous Sequence ◽  
Rabbit Immunoglobulin

A partial amino acid sequence was given by Cebra, Steiner & Porter (1968b) of the N-terminal half of the heavy chain of rabbit immunoglobulin G. This was extended and in part corrected to give a continuous sequence of 136 residues, which together with other work accounts for three-quarters of the total sequence. Evidence is given suggesting that there is a limited region of 10–15 residues that are exceptionally variable in the heavy chains from pooled rabbit immunoglobulin G.

Studies on the amino acid sequence of heavy chains from rabbit immunoglobulin G

1966 ◽  
Vol 166 (1003) ◽  
pp. 159-175 ◽  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Light Chains ◽  
Antibody Specificity ◽  
Sequence Heterogeneity ◽  
Specific Antibodies ◽  
Heavy Chains ◽  
Insight Into

It is now generally agreed that the four-chain subunit structure of Immunoglobulins which was first proposed by Porter (1962), accurately represents the gross structure of immunoglobulin G (IgG) and specific antibodies (Fleischman, Porter & Press 1963; Edelman & Gally 1964; Marler, Nelson & Tanford 1964; Nelson et al . 1965). However, an understanding of the structural basis of antibody specificity requires greater insight into the amino acid sequence of the polypeptide chain components of specific antibodies. Isolated light chains from specific antibodies and inert IgG, show a considerable degree of electrophoretic heterogeneity (Edelman & Gally 1964; Cohen & Porter 1964; Poulik 1964). Tryptic peptide maps of light chains (Nelson et al . 1965) have suggested that this heterogeneity may be accounted for by differences in amino acid sequence. This view has received considerable support from the observation that Bence-Jones proteins, which may be regarded as light chains, vary significantly in amino acid sequence (Hilschman & Craig 1965; Milstein 1966; Titani, Whitley & Putman 1966). A similar but less well-defined sequence heterogeneity has been suggested to exist in the heavy chains of specific antibodies (Feinstein 1964). However, the Fc fragment of the heavy chains has been thought to possess a regular amino acid sequence which may be similar, if not identical, among all specific antibodies (Porter 1959; Nelson et al . 1965). This paper summarizes the results of studies on the amino acid sequence of heavy chains and that portion of heavy chain, Fc fragment, which is obtained on treatment of rabbit IgG with papain (Porter 1959). These studies were designed to determine how much of the amino acid sequence of heavy chain could be accounted for by a unique, regular amino acid sequence which was common to most, if not all, IgG antibodies. In addition, attempts were made to locate regions of heavy chains which varied in amino acid sequence. Although structural variants appear to occur among the heavy chains found in non-specific IgG, it would be desirable to know what portion of the heavy chain sequence is invariant among all antibodies. If antibody specificity results from sequence heterogeneity in light and heavy chains, then knowledge of the variant and invariant portions of these chains may provide insight into the nature of specific binding sites in anti-­bodies.

scholarly journals The partial sequence of two large peptides from the N-terminal half of heavy chains from normal rabbit immunoglobulin G

1968 ◽  
Vol 107 (1) ◽  
pp. 79-88 ◽  
Author(s):  
J. J. Cebra ◽  
L. A. Steiner ◽  
R R Porter
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Immunoglobulin G ◽  
Preceding Paper ◽  
Rabbit Serum ◽  
Normal Rabbit Serum ◽  
Heavy Chains ◽  
Rabbit Immunoglobulin ◽  
Terminal Section

The partial amino acid sequence of two large peptides is described. These were prepared from the N-terminal half of the heavy chain of immunoglobulin G from pooled normal rabbit serum by tryptic digestion after the ∈-amino groups of the lysine residues had been blocked with S-ethyl trifluorothioacetate. These peptides are believed to account for about 145 residues of fragment C-1, the N-terminal section of rabbit immunoglobulin G heavy chain prepared by cyanogen bromide cleavage. The evidence from the present paper and the preceding paper (Cebra, Givol & Porter, 1968) suggests that it may be possible to deduce a predominant amino acid sequence for most, if not all, of this section of the molecule.

Amino Acid Sequence of the Amino-Terminal 24 kDa Fragment of the Heavy Chain of Chicken Gizzard Myosin1

1987 ◽  
Vol 102 (1) ◽  
pp. 133-145 ◽  
Author(s):  
Tetsuo MAITA ◽  
Hirofumi ONISHI ◽  
Eiko YAJIMA ◽  
Genji MATSUDA
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Chicken Gizzard ◽  
Amino Terminal

The Complete Amino-Acid Sequence of the Heavy Chain of the Human Myeloma Protein WIE, an Immunoglobulin D

1991 ◽  
Vol 372 (2) ◽  
pp. 795-818 ◽  
Author(s):  
R. Joachim FRIEDRICH ◽  
Rolf BÄTGE ◽  
Iris SCHRANNER ◽  
Ulrike KOTUCHA ◽  
Klaus ECKART ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Myeloma Protein ◽  
Complete Amino Acid Sequence ◽  
Immunoglobulin D
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