The covalent structure of a human γG-immunoglobulin.  II.  Isolation and characterization of the cyanogen bromide fragments

Waxdal, Myron J.; Konigsberg, William H.; Henley, Walter L.; Edelman, Gerald M.

doi:10.1021/bi00845a046

Cited by 174 publications

(70 citation statements)

References 19 publications

(27 reference statements)

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“…This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. Amino acid sequence analysis of the fully reduced and alkylated protein (24) was carried out in the automatic sequencer (Beckman 890C) using the Quadrol double cleavage program. Residues released were identified by thin-layer chromatography (25), by back hydrolysis in 6 M HCI under reduced pressure for 24 hr at 1500 followed by amino acid analysis, and by colorimetric assay (His and Arg) (26,27).…”

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confidence: 99%

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Crystallographic studies of bovine beta2-microglobulin.

Becker¹,

Ziffer²,

Edelman³

et al. 1977

Proc. Natl. Acad. Sci. U.S.A.

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Crystals of the bovine milk protein lactollin yield x-ray diffraction data extending to a resolution of 2.8 A.Lactollin is a bovine analogue of #2-microglobulin, a protein that is homologous in amino acid sequence to the constant domains of immunoglobulins and is the light chain of the human and murine major histocompatability antigens. The protein crystallizes in the orthorhombic space group P212121 with a = 77.4, b = 47.9, and c = 34.3 A. The #2-Microglobulin is a protein distinguished by its similarity to certain portions of immunoglobulins (1-3) and by its association on cell surfaces with the major histocompatability antigens of man (HLA) and mouse (H-2) (4-7). Since its discovery in human urine in 1968, the overall properties, synthesis, and amino acid sequence of this protein have been characterized (2,(8)(9)(10)(11). Similar proteins have been detected in a variety of species, and all appear as a single polypeptide [molecular weight (Mr) = 11,600], with few differences in amino acid sequence among the proteins from different species (2,3,(12)(13)(14).Comparison of the amino acid sequence and other features of human #32-microglobulin with immunoglobulins (1, 15) has indicated that it closely resembles the constant homology regions (16) of immunoglobulins G, M, and E. In intact immunoglobulin molecules, each homology region is closely associated with the corresponding homology region of another immunoglobulin chain in pairs of domains (16, 17), whereas ,62-microglobulin is found associated with the heavy chain of HLA or H-2 antigens or the closely related thymus leukemia antigen (4-7, 18, 19), suggesting that such paired domains may be structural features of these cell surface molecules. In solution,purified Or-microglobulin, however, is generally unpaired; i.e., it appears as a free monomer (8) The elucidation of the three-dimensional structure of ,32-microglobulin would be of particular interest because it would provide an opportunity to compare this molecule in detail with immunoglobulin domains, and thus contribute to an understanding of its interaction with the heavy chains of H-2 and HLA antigens. It has recently been found that lactollin, a crystalline protein isolated from bovine milk and colostrum, has an amino-terminal amino acid sequence sufficiently similar to those of 6B2-microglobulins from several species to indicate that it is probably a bovine homologue of the protein (M. L. Groves, private communication; refs. 20 and 21). Although the reported molecular weight of lactollin is 43,000 (22), it is composed of subunits of 12,000 daltons. We have confirmed the molecular weight of the subunit and the similarity in amino acid sequence to 62-microglobulin. We report here x-ray diffraction studies ofThe costs of publication of this article were defrayed in part by the payment of page charges from funds made available to support the research which is the subject of the article. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. Amino acid sequence ana...

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confidence: 99%

“…To compare tryptic peptides, 0.5 mg of fully reduced and alkylated (24) (22) on Sephadex G-75 in phosphate-buffered saline; the column was calibrated with blue dextran (BD), ovalbumin (OA), cytochrome c (CC), human f2-microglobulin (HA2), and phenol red (PR). using NaCl.…”

mentioning

confidence: 99%

Crystallographic studies of bovine beta2-microglobulin.

Becker¹,

Ziffer²,

Edelman³

et al. 1977

Proc. Natl. Acad. Sci. U.S.A.

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“…of SOD Reduction and S-carboxymethylation were carried out as described by WAXDAL et al (30). Typically, 60 mg (3.8 ~moles of subunit) of SOD were dissolved in 6 ml of 0.5 M-Tris-HC1 buffer pH 9.0, containing 0.002 M-ethylenediamine tetraacetate, and 6 M-guanidine hydrochloride.…”

Section: Reduction and S-carboxymethylationmentioning

confidence: 99%

The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae

Johansen

Overballe-Petersen

Martin

et al. 1979

Carlsberg Res. Commun.

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The amino acid sequence of the copper,zinc superoxide dismutase from Saccharomyces cerevisiae has been determined by automated Edman degradation. Peptides were obtained from cyanogen bromide cleavage, Staphylococcus aureus V8 protease digestion, tryptic and chymotryptic digests of the citraconylated reduced and carboxymethylated enzyme, and by further fragmentation of selected peptides with trypsin. From the alignment of these peptides and the previously published sequence of the first 54 amino terminal residues (24) the complete sequence was deduced by direct sequence identification of all 153 amino acid residues and of all peptide overlaps. The amino acid sequence corresponds to a molecular weight of 15,950 for each of the two identical subunits in the native enzyme. The primary structure of yeast copper, zinc superoxide dismutase is 55 96 identical with the sequence of the copper, zinc enzyme from bovine erythrocytes. Importantly, all the copper and zinc ligands, six histidine residues and one aspartate residue from the bovine enzyme, are conserved in the ye,~st enzyme. The high overall sequence homology and conservation of important metal binding active site amino acid residues suggest that the three-dimensional structure and in particular the active site geometry is virtually the same for the bovine and yeast enzyme. In contrast no sequence homology is apparent by comparison with the manganese or iron class of superoxide dismutases indicating that the two classes have not evolved from a common ancestor. Superoxide dismutases (SOD) are a group of metalloenzymes, whose function is to scavenge the superoxide radical anion 02 (12) by catalyzing its dismutation to hydrogen peroxide and dioxygen:

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“…The procedure of Waxdal et al [23] was followed. Exchange protein (25 mg) was dissolved in 2 ml of 0.5 M Tris .…”

Section: Cl~emical Modijications Of the Exchange Proteinmentioning

confidence: 99%

The Primary Structure of the Phosphatidylcholine‐Exchange Protein from Bovine Liver

Moonen

Akeroyd

Westerman

et al. 1980

European Journal of Biochemistry

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The phosphatidylcholine exchange protein from bovine liver consists of a single polypeptide chain and has a blocked N terminus. The protein contains an estimated 244 amino acid residues in accordance with a determined molecular weight of 28 000. The protease from mouse submaxillaris gland cleaved the citraconylated and S-carboxymethylated derivative of the exchange protein at one specific site (Argl4-GluI5) close to the N terminus. Analysis of the two resulting peptides showed that N-acetyl-methionine was the N-terminal residue and gave the sequence of the first 41 residues.The modified protein was also fragmented with the protease from Staphylococcus aureus. The peptides isolated represented 88 of the protein; their sequences were determined by manual and automated Edman degradation. Alignment of a number of these peptides gave the complete sequence of the N-terminal half up to position 322.Phospholipid exchange proteins catalyze the transfer of phospholipids between membranes. A number of these proteins, different in molecular weight, isoelectric point and transfer specificity, have been isolated from bovine liver [l], heart [2,3] and brain [4,5], rat liver [6 -81, small intestinal mucosa [9] and hepatoma [lo], sheep lung [ l l ] and potato tuber [12]. To date, three general classes of exchange proteins can be distinguished, that is the phosphatidylcholinespecific exchange protein [1,6,9,11], the exchange proteins that display a great preference for phosphatidylinositol [4 -6,9] and the non-specific exchange proteins [8, lo]. These proteins range in molecular weight between 10000 and 35000 and in isoelectric point between pH 5 and 9.

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The covalent structure of a human γG-immunoglobulin. II. Isolation and characterization of the cyanogen bromide fragments

Cited by 174 publications

References 19 publications

Crystallographic studies of bovine beta2-microglobulin.

Crystallographic studies of bovine beta2-microglobulin.

The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae

The Primary Structure of the Phosphatidylcholine‐Exchange Protein from Bovine Liver

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