Comparative analysis of the IgG heavy chain carbohydrate peptide

Howell, Jeanne M.; Le, Hood; Sanders, Brenda Μ.

doi:10.1016/s0022-2836(67)80044-5

Cited by 21 publications

(7 citation statements)

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“…The sequence around the site of attachment of the carbohydrate on Cor Fd fragment is Tyr-Asx-Thr-Ser, which is very similar to the sequence around the carbohydrate oIn the Fc f ragment of human and rabbit heavy chains, namely Tyr-Asn-Ser-Thr and Phe-Asx-Ser-Thr (Edelinan et Hill, Delaney, Fellows, & Lebovitz, 1966) and on the moutse light chain, Gln-Asx-Ile-Ser (Melchers, 1969). Comparison of glycopeptides from heavy chains of several species is consistent with the sequence -Asx(CHO)-X-Ser (Thr)as the site of attachment of carbohydrate, where X can be one of several amino acids (Howell, Hood & Sanders, 1967), and it was suggested by Neuberger & Marshall (1968) that this sequence might be a recognition site for an enzyme involved in the attachment of hexosamine to proteins. However, bovine ribonuclease B contains a carbohydrate moiety attached to an aspartic residue, whereas in ribonuclease A the sarne sequence occurs, namely Asn-Leu-Thr-Lys, without any carbohydrate attached (Plummer & Hirs, 1964).…”

Section: Discussionsupporting

confidence: 68%

The amino acid sequences of the Fd fragments of two human γ 1 heavy chains

Press

Hogg

1970

Biochemical Journal

105

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The amino acid sequences of the Fd fragments of two human pathological immunoglobulins of the immunoglobulin G1 class are reported. Comparison of the two sequences shows that the heavy-chain variable regions are similar in length to those of the light chains. The existence of heavy chain variable region subgroups is also deduced, from a comparison of these two sequences with those of another gamma 1 chain, Eu, a mu chain, Ou, and the partial sequence of a fourth gamma 1 chain, Ste. Carbohydrate has been found to be linked to an aspartic acid residue in the variable region of one of the gamma 1 chains, Cor.

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Section: Discussionsupporting

confidence: 68%

The amino acid sequences of the Fd fragments of two human γ 1 heavy chains

Press

Hogg

1970

Biochemical Journal

105

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“…After three steps of Edman degradation, carbohydrate was still present on the residual peptide. Also, digestion with carboxypeptidases A and B released the four carboxy terminal residues, leaving only the Asx at position 297 as the point of attachment for the carbohydrate, in correspondence with other immunoglobulin heavy chains (Howell et al, 1967;Hunt and Dayhoff, 1970). The presence of homoserine and its lactone identified peptide T-3 as the carboxy terminal tryptic peptide of fragment H-5.…”

Section: Resultsmentioning

confidence: 99%

“…A precise determination of the charge on residue 297 was not possible because of the attachment of acidic carbohydrate at this point. This asparaginyl residue is a common site of carbohydrate attachment in IgG immunoglobulins (Howell et al, 1967; Hunt and Dayhoff, 1970).…”

Section: Resultsmentioning

confidence: 99%

Amino acid sequence of a murine immunoglobulin fragment that possesses complement fixing activity

Kehoe¹,

Bourgois²,

Capra³

et al. 1974

Biochemistry

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The amino acid sequence of 62-residue cyanogen bromide fragment located in the Fc region of a murine IgG2a immunoglobulin has been determined using a combination of automated and manual Edman degradation techniques. This fragment, which comprises the major portion of the IgG Ch2 domain, had previously been shown capable of fixing a significant quantity of guinea pig complement when bound to polystyrene latex particles. The sequence was compared with those available for the corresponding region of other immunoglobulins from man, the rabbit, and the guinea pig. The various interspecies sequence comparisons showed that sequence identities for the part of the mammalian IgG T A he functional duality of immunoglobulin molecules is now well established. A primary function, antigen binding, is carried out by variable regions of both light and heavy polypeptide chains, while the biological, or effector, properties are mediated by heavy chain constant regions (Edelman and

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“…This Fc portion of the constant region of heavy chains can be crystallized and has been shown to play a part in physiological functions of yG immunoglobulin such as skin fixation, placental transfer, and complement fixation.9 Studies on the amino acid sequence1 of Fc fragments from pooled rabbit yG immunoglobulin have provided the basis for the hypothesis that the whole immunoglobulin molecule has evolved by successive duplications of a gene that originally was approximately 300 nucleotides long. 11 Recently we have determined the amino acid sequence of the Fc portion of the human myeloma protein Eu and in the present communication compare this sequence with other regions of the same immunoglobulin molecule5' 6 as well as with sequences of other human and animal immunoglobulin chains.8' [12][13][14] Three stretches, at the beginning, middle, and end of the Fc regions, were found to be almost identical in rabbit and human yG immunoglobulin. The results extend the homologies established among constant regions of immunoglobulin sequences and provide the basis for the mapping of active sites as well as the precise location'4 of amino acids determined by Gm loci.…”

mentioning

confidence: 73%