Immunoglobulin Lambda Chain Structure: Two Genes, One Polypeptide Chain

LEROY HOOD; DANIEL EIN

doi:10.1038/220764a0

The subunit and polypeptide-chain structure of rabbit secretory immunoglobulin A. Isolation of a proteolytic fragment suitable for sequence studies on the variable region of α-chain

Biochemical Journal ◽

10.1042/bj1670245 ◽

1977 ◽

Vol 167 (1) ◽

pp. 245-253 ◽

Cited By ~ 2

Author(s):

A P Johnstone ◽

L E Mole

Keyword(s):

Immunoglobulin G ◽

Polypeptide Chain ◽

Immunoglobulin A ◽

Variable Region ◽

Chain Structure ◽

Secretory Immunoglobulin A ◽

Primary Sequence ◽

Relative Resistance ◽

Proteolytic Fragment ◽

Secretory Immunoglobulin

A method was developed for the preparation of a proteolytic fragment of rabbit secretory immunoglobulin A (sIgA) which contains the variable region of the alpha-chain; this fragment is suitable for primary-sequence studies. The serologically defined subclasses of sIgA are shown to correlate partially with the nature of the binding of a constituent chain of sIgA, called secretory piece. Data are also presented on the relative resistance of sIgA to enzymic and reductive cleavage, compared with immunoglobulin G.

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Variations in the heavy polypeptide chain structure of gamma myeloma immunoglobulins from an inbred strain of mice and a hypothesis as to their origin

Journal of Molecular Biology ◽

10.1016/s0022-2836(65)80187-5 ◽

1965 ◽

Vol 14 (2) ◽

pp. 361-IN6 ◽

Cited By ~ 49

Author(s):

Michael Potter ◽

Ettore Appella ◽

Seymour Geisser

Keyword(s):

Inbred Strain ◽

Polypeptide Chain ◽

Chain Structure

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The membrane attack mechanism of complement: the three polypeptide chain structure of the eigth component (C8).

Journal of Experimental Medicine ◽

10.1084/jem.143.5.1131 ◽

1976 ◽

Vol 143 (5) ◽

pp. 1131-1139 ◽

Cited By ~ 70

Author(s):

W P Klob ◽

H J Müller-Eberhard

Keyword(s):

Ion Exchange ◽

Human Serum ◽

Ammonium Sulfate ◽

Gel Electrophoresis ◽

Polypeptide Chain ◽

Polyacrylamide Gel Electrophoresis ◽

Chain Structure ◽

Ammonium Sulfate Precipitation ◽

Ion Exchange Column ◽

Polypeptide Chains

The purification of human C8 in milligram quantities from outdated human serum was achieved by ammonium sulfate precipitation (37.5-50% saturation) and ion exchange column chromatography employing CM-32 cellulose and QAE-Sephadex. The yield of C8 activity ranged from 2-9%, and the average purification was 1,700-fold. Fully reduced C8 was shown by SDS polyacrylamide gel electrophoresis to have three polypeptide chains which were present in equimolor ratios: alpha, 77,000 daltons; beta, 63,000 daltons; and gamma, 13,700 daltons. C8 denaturation by SDS and urea in the absence of reducing agents revealed two noncovalently linked subunits: alpha-gamma, 99,000 daltons, and beta, 75,000 daltons.

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Polypeptide chain structure of sting ray immunoglobulin

Biochimica et Biophysica Acta (BBA) - Protein Structure ◽

10.1016/0005-2795(70)90232-1 ◽

1970 ◽

Vol 221 (3) ◽

pp. 604-611 ◽

Cited By ~ 23

Author(s):

John J. Marchalonis ◽

Steven A. Schonfeld

Keyword(s):

Polypeptide Chain ◽

Chain Structure

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A Soluble Fibrin Standard: Comparable Dose-response with Immunologic and Functional Assays

Thrombosis and Haemostasis ◽

10.1055/s-0037-1614644 ◽

1999 ◽

Vol 82 (07) ◽

pp. 145-148 ◽

Cited By ~ 5

Author(s):

Victor Marder ◽

Joel Kanouse ◽

Charles Francis ◽

Bonnie McCarron

Keyword(s):

Dose Response ◽

Polypeptide Chain ◽

Chain Structure ◽

Latex Agglutination ◽

Soluble Fibrin ◽

Functional Assays ◽

Parallel Lines ◽

Sds Page ◽

Immunologic Reactions

SummaryA soluble fibrin (SF) preparation has been developed as a potential standard by the Scientific and Standardization Committee for use in assays evaluating in vitro preparations and patient plasma samples. The SF standard was prepared by reaction of factor XIII-free fibrinogen with thrombin, followed by neutralization with hirudin and solubilization of the fibrin in acetic acid. As characterized by SDS-PAGE, the polypeptide chain structure shows the anticipated loss of fibrinopep-tides and lack of sγ or α chain crosslinking. The standard was added to pooled normal plasma at concentrations from 12.5 μg/ml to 340 μg/ml and tested with four commercially available assays based on immunologic reactions using ELISA or latex agglutination or on t-PA cofactor activity for plasminogen to plasmin conversion. Absolute “soluble fibrin” concentrations were calculated using the manufacturers’ calibrators and showed distinct dose-response relationships for each assay. Expression of the results following log-transformation produced a series of parallel lines, indicating that this SF preparation can serve as a standard, effectively normalizing the disparate proprietary internal calibrators currently used for each assay.

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Polypeptide Chain Structure of Inter-α-Trypsin Inhibitor and Pre-α-Trypsin Inhibitor: Evidence for Chain Assembly by Glycan and Comparison with other “Kunin”-Containing Proteins

Serine Proteases and Their Serpin Inhibitors in the Nervous System ◽

10.1007/978-1-4684-8357-4_8 ◽

1990 ◽

pp. 79-91 ◽

Cited By ~ 1

Author(s):

Jan J. Enghild ◽

Ida B. Thørgersen ◽

Salvatore V. Pizzo ◽

Guy Salvesen

Keyword(s):

Trypsin Inhibitor ◽

Polypeptide Chain ◽

Chain Structure

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Polypeptide chain configurations in crystalline proteins

Proceedings of the Royal Society of London Series A - Mathematical and Physical Sciences ◽

10.1098/rspa.1950.0142 ◽

1950 ◽

Vol 203 (1074) ◽

pp. 321-357 ◽

Cited By ~ 105

Keyword(s):

General Type ◽

Polypeptide Chain ◽

Three Dimensional ◽

Chain Structure ◽

Two Dimensional ◽

Amino Acid Residues ◽

Intensive Study ◽

Repeat Distance ◽

X Ray

Astbury’s studies of α-keratin, and X-ray studies of crystalline haemoglobin and myoglobin by Perutz and Kendrew, agree in indicating some form of folded polypeptide chain which has a repeat distance of about 5·1 Å, with three amino-acid residues per repeat. In this paper a systematic survey has been made of chain models which conform to established bond lengths and angles, and which are held in a folded form by N—H—O bonds. After excluding the models which depart widely from the observed repeat distance and number of residues per repeat, an attempt is made to reduce the number of possibilities still further by comparing vector diagrams of the models with Patterson projections based on the X-ray data. When this comparison is made for two-dimensional Patterson projections on a plane at right angles to the chain, the evidence favours chains of the general type proposed for a-keratin by Astbury. These chains have a dyad axis with six residues in a repeat distance of 10·2 Å, and are composed of approximately coplanar folds. As a further test, these chains are placed in the myoglobin structure, and a comparison is made between calculated and observed F values for a zone parallel to the chains; the agreement is remarkably close taking into account the omission from the calculations of the unknown effect of the side-chains. On the other hand, a study of the three-dimensional Patterson of haemoglobin shows how cautious one must be in accepting this agreement as significant. Successive portions of the rod of high vector density which has been supposed to represent the chains give widely different projections and show no evidence of a dyad axis. The evidence is still too slender for definite conclusions to be drawn, but it indicates that a further intensive study of these proteins, and in particular of myoglobin which has promising features of simplicity, may lead to a determination of the chain structure.

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An X-ray study of horse methaemoglobin. II

Proceedings of the Royal Society of London Series A - Mathematical and Physical Sciences ◽

10.1098/rspa.1949.0005 ◽

1949 ◽

Vol 195 (1043) ◽

pp. 474-499 ◽

Cited By ~ 39

Keyword(s):

Short Range ◽

Polypeptide Chain ◽

Average Distance ◽

Three Dimensional ◽

Chain Structure ◽

Closed Loops ◽

X Ray ◽

Vector Density ◽

Polypeptide Chains ◽

Haemoglobin Molecule

A complete three-dimensional Patterson synthesis of haemoglobin has been calculated, giving the distribution of vector density in thirty-one sections through the unit cell. The sections show certain concentrations of vector density which can be interpreted in terms of polypeptide chain structure. The following are the conclusions tentatively arrived at on the evidence described in this paper. The haemoglobin molecule resembles a cylinder of 57 Å diameter and 34Å height, which consists of an assembly of polypeptide chains running parallel to the base of the cylinder. The chains show a short-range fold, with a prominent vector of 5 Å parallel to the chain direction. In addition to this the chains also contain a longer fold which may extend through the whole width of the molecule. This long fold may be due either to open chains folded backwards and forwards through the molecule or to closed loops of polypeptide chains. The average distance between neighbouring chains, or neighbouring portions of the same chain folded back on itself, is 10.5 Å. The chains are arranged in four layers which are about 9 Å apart and correspond to the four layers of scattering matter described in a previous paper. The haem groups lie with their flat sides approximately normal to the chain direction.

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