Differences in the Amino Acid Composition of a Third Rabbit Antibody

Koshland, Marian Elliott; Englberger, Frieda M.; Shapanka, Roslyn

doi:10.1126/science.143.3612.1330

Cited by 22 publications

(16 citation statements)

References 5 publications

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“…This numerical estimate is consistent with data by Koshland et al [18,19] on differences in the aminoacid composition of purified anti-hapten antibodies of completely unrelated specificity. An antibody recognition site of the approximate composition Arg3 Iluj Tyr3 seems to be complementary to the negatively charged p-azobenzene arsonic acid hapten; and Arg, Asp3 IlUi seems to be sterically complementary to p-azo-(3-phenyllactoside hapten.…”

Section: Antigenic Determinant Amino Acyl Residuessupporting

confidence: 81%

An Information Transfer Hypothesis of the Immune Response Based on the Genetic Code

Carvalho¹,

Schultz²

1971

Oncology

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A new instructive type hypothesis has been formulated to account for the flow of information from an antigenic determinant to the corresponding recognition site in an antibody. It is postulated that antigen in the macrophage is broken down into determinant fragments containing about 5 aminoacyl residues. These residues attract a complementary sequence of aminoacyl groups attached to their respective s-RNA molecules, whose anticodons serve as a template for the formation of a short strand of antigenically informed RNA or cRNA. This cRNA, or its double stranded form c₂ RNA is hybridized with genomic DNA from which a cDNA results. This c₂DNA is integrated as a contiguous codon sequence into the lymphocyte gene coded for the l-chain of IgG. Synthesis of this chain and assembly of the antibody then proceeds in conventional ways and means. Hybridization of cRNA-DNA is probably the mechanism of immunologic selrecognition. This concept leads to the corolary of a symmetrical arrangement of the genetic code, including its degeneracy and redundancy. The arrangement suggests that antigen-antibody recognition is mediated by a complementary relationship between the following pairs of aminoacids: Phe-Lys, Leu-AspN, Leu-Glu, Lau-Asp, Ilu-Tyr, Meth-Tyr, Val-Glu, Val-His, Ser-Arg, Ser-Ser, Pro-Gly, Thr-Tyr, Thr-Cys and Ala-Arg.

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Section: Antigenic Determinant Amino Acyl Residuessupporting

confidence: 81%

An Information Transfer Hypothesis of the Immune Response Based on the Genetic Code

Carvalho¹,

Schultz²

1971

Oncology

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Section: Discussionmentioning

confidence: 68%

“…Previous reports have indicated that amino acid differences may be found between antibodies of different specificities isolated from single rabbits (7,9). The am{no acid composition of these antibodies did not vary according to the allotype of animal (9). It was inferred (7) that these residue differences were complementary in terms of numbers of acidic and basic amino acids, to the basic and acidic haptenic antigens which were used for antibody induction.…”

Section: Discussionmentioning

confidence: 92%

“…Antibodies with four different specificities, as well as 7G-globulin were analyzed. Differences of from 7 to 32 residues were found from one antibody to another for the amino acids listed in Table II, as compared with maximum variation of eight amino acids found with the three different rabbit antibodies (7,9,10). The Gm Groups of these human antibodies are also known and although the 7G from the individual studied was Gm (a + b +), three of the antibodies were Gm (a --b --) and one, (anti-A) was Gm (a + b --).…”

Section: Discussionmentioning

confidence: 93%

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Studies on Human Antibodies

Bassett

Tanenbaum

Pryzwansky

et al. 1965

The Journal of Experimental Medicine

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The amino acid composition of pooled human 7-globulin was studied comprehensively by Brand and coworkers (1). More recent studies of 6.5S human globulins, now called 7G-globulin (2), using automatic zmlno acid analytical techniques (3), have been reported for example, by Hsaio and Putnam (4), and by Crumpton and Wilkinson (5). In contrast to the situation with amino acid analyses of specific antibodies from the rabbit (5-10), the residue composition of human antibody 3,-globulins to well defined antigens, especially from individual subjects, has yet to be investigated. This paper is concerned with a study of the amino acid composition of four purified 7G-antibodies, namely antilevan, antidextran, antiteichoic acid, and antiblood group substance A, from the serum of one individual. These four antibody preparations were previously examined for their allotypic speciiicities (11) and for the electrophoretic patterns of their H and L chains in starch gel (12).As has previously been reported by Koshland et al. for rabbit antibodies to several antigens (7-9), analytically significant differences in amino acid composition among these purified human antibodies have also been observed. Thus, there is wide variation in the number of glycine, valine, leucine, proline, threonine, tyrosine, and arginlne residues in these "yG-antibodies, as well as smaller differences in other amino acid residues. Furthermore, hydroxTlysine is present in antidextran and in antiteichoic acid whereas it cannot be detected in antilevan, anti-A, or in the normal non-specific "~,G-globulin from this subject. Materials and MethodsPreparation of'yG.--Serum from subject 1 (11, 12) was dialyzed against several changes of 0.01 ,s potassium phosphate buffer, pH 7.2. It was then subjected to chromatography (13) on a DEAE-cellulose column (75 X 2.5 cm) which had previously been equilibrated with this buffer. The "yG-fraction was eluted as the first protein peak in the effluent, and was dialyzed

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“…Studies on the amino acid composition of purified antibodies were first carried out by K o s h l a n d (116,117) who showed that significant analytical differences in a number of amino acids oc curred among three different antibodies, one to a positively charged (ammonium), one to a negatively charged (arsonic acid) and one to a neutral sugar (Lac) determinant; antibodies to two of the anti gens were formed in single rabbits. Results in Table I show the amino acids in which differences were found.…”

Section: S Tructure and H Eterogeneity Of A Ntibodies* Ea K A B A Tmentioning

confidence: 99%

Structure and Heterogeneity of Antibodies

Kabat¹

1966

Acta Haematol

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Differences in the Amino Acid Composition of a Third Rabbit Antibody

Cited by 22 publications

References 5 publications

An Information Transfer Hypothesis of the Immune Response Based on the Genetic Code

An Information Transfer Hypothesis of the Immune Response Based on the Genetic Code

Studies on Human Antibodies

Structure and Heterogeneity of Antibodies

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