The little tea book / compiled by Arthur Gray ; illustrated by George W. Hood

Gray, Arthur; Hood, George W.

doi:10.5962/bhl.title.21955

Cited by 9 publications

(15 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1). Two-dimensional electrophoresis a t pH 3.5 (Fig.4) of the material contained in this peak allowed further purification of two peptides (XI P and %I1 P), the amino acid composition of which appears in Table 1, that could be assigned to XI and xII cysteine-containing peptides by homology with other reported sequences of the mouse chains [6,21]. The final yield of these peptides was extremely low, so that direct sequence determination could not be achieved.…”

Section: Intrachain Bridges Of the Light Chainsmentioning

confidence: 90%

“…Representation of the hd{-molecule MOPC 173 showing the sequences determined i n the Vicinity of cysteine residues.Numbering for the heavy chain (71 to 7x11 cysteine) is that of Eu [S] and MOPC 173[2]. Numbering for the light chain (XI to xV) cysteine is taken from[6,21] Topological model of ,the? MOPC 173 yC2a mouse immunoglobulin indicating the cyanogen bromide fragments and the general pattern of disulfide bonds…”

mentioning

confidence: 99%

See 1 more Smart Citation

Determination of the Primary Structure of a Mouse γG2a Immunoglobulin Identification of the Disulfide Bridges

Préval

Fouegreau

1972

European Journal of Biochemistry

View full text Add to dashboard Cite

All cysteine‐containing peptides of the MOPC 173 (γG2a) monoclonal immunoglobulin were isolated and sequenced, allowing characterization of the twelve intrachain disulfide bonds, and extension of previous work concerning the interchain disulfide bridges [3]. Positioning of the various bonds was deduced from homology with the known sequences of the mouse x chains [6,21], MOPC 173 VH region [2], and human γ chains [8], and allowed corroboration of the previous proposed order of the CNBr fragments isolated from the whole molecule [1]. The general pattern of the γG2a mouse immunoglobulin seems in agreement with the accepted view that this molecule contains two heavy chains and two light chains linked by disulfide bonds, and having intrachain bridges disposed in a strictly linear manner [4,8].

show abstract

Section: Intrachain Bridges Of the Light Chainsmentioning

confidence: 90%

mentioning

confidence: 99%

Determination of the Primary Structure of a Mouse γG2a Immunoglobulin Identification of the Disulfide Bridges

Préval

Fouegreau

1972

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…So far, extensivc sequence studies have been published for six murine monoclonal x light chains [27-301, of which three constant regions were entirely (MOPC 21 [28] or partially (MOPC 41 [27] and MOPC 321 [29]) determined. Minor amino acid differences have been reported in the sequences of the C-region [29], at positions 161 and 165 between MOPC 321 and MOPC 21, and at positions 127 and 129, between MOPC 21 and MOPC 41, although data for the MOPC 41 protein were only partial.…”

Section: Discussionmentioning

confidence: 99%

“…Nevertheless, differences observed with proteins MOPC 41 [27] and MOPC 321 [29], would be suggestive of a duplication event, if, as pointed out by McKean etal. [29].…”

mentioning

confidence: 95%

See 1 more Smart Citation

Determination of the Primary Structure of a Mouse IgG2a Immunoglobulin

Schiff¹,

Fougereau²

1975

European Journal of Biochemistry

View full text Add to dashboard Cite

The amino acid sequence of the light chain of the mouse monoclonal MOPC 173 immunoglobulin molecule (IgG2a,x) is presented. This kappa chain contains 214 residues. Comparisons of this sequence with murine kappa chains already published by other workers bring a confirmation of the large size of the murine Vx chain pool. A complete identity was found with the constant region of the light chain of MOPC 21 from residue 97 to residue 214.We have undertaken the determination of the complete amino acid sequence of the murine MOPC 173 immunoglobulin molecule, which is a monoclonal protein of the IgG2a (x) class [I]. A topological model of the molecule has been proposed, on the grounds of results derived from the isolation and characterization of the CNBr fragments of the entire molecule [2], and from the identification of the interchain and intrachain disulfide bridges [3,4]. The sequence of the CNBr fragments H1, H2, H3 (covering most of the V, region), and that of fragments H5 to H10, accounting for the hinge region and the Fc fragment have already been published [5 -71.We report in the present paper the amino acid sequence of the light chain of this molecule. MATERIALS AND METHODS Isolation of the MOPC 173 ProteinPlasmacytomas which originated from Dr Potter's laboratory, were serially transplanted in Balb/c mice, in solid form, by subcutaneous injection of small tumor fragments. On the average, mice were bled three weeks after the transplantation. The immunoglobulin fraction of pooled sera was precipitated with ammonium sulfate (33 % saturation, final concentration), and was further purified by chromatography on DEAE cellulose (DE 52, Whatman) equilibrated with 0.017 M phosphate buffer (pH 7.3). Purity was checked by immunoelectrophoresis [8], using a rabbit antiserum against whole Balb/c mouse serum. Isolation of the Light ChainsThe MOPC 173 immunoglobulin molecule (500mg) was mildly reduced in 0.1 M Tris buffer, 0.15 M NaC1, 0.002 M EDTA, pH 8.2, with dithiothreitol (Calbiochem), according to Frangione et al. [9] (except that the molarity of the reagent was 8 mM) and alkylated with a 2.5 molar excess of iodoacetamide. Chains were then separated by gel-filtration on a Sephadex G-100 superfine column ( 5 x 100 cm) equilibrated in 1.0 M propionic acid. Purity of the light chains was tested by polyacrylamide (7.5 %) gel electrophoresis according to Shapiro and Maize1 [lo].Complete reduction and alkylation of the isolated light chains was made according to Waxdal et al.[ 1 1 1.except that 8 M urea was used instead of guanidine. Whenever labelled peptides were required, alkylation was performed, according to Frangione et al. [9], by making the reduced solution 0.02 M with iodo['"C]acetic acid (Amersham), using a 0.1 M stock solution (specific activity 83 pCi/ml). Radioactivity was counted in a Packard spectrometer 3380. Isolation of the CNBr FragmentsCNBr fragments were prepared by direct attack of the whole MOPC 173 molecule. Fragments L1 and L3 were isolated by successive steps of gel filtration, as previously descri...

show abstract

Towards improved radar estimates of surface precipitation rate at long range

Kitchen

1997

Quart J Royal Meteoro Soc

View full text Add to dashboard Cite

A method has been developed for estimating surface precipitation rates using reflectivities measured with a radar scanning at several different angles of elevation. In each pixel of a radar image, an idealized profile of the reflectivity factor is constructed. Each profile is defined in terms of three unknowns: the reflectivity in the rain beneath the melting layer, and the slope of the profile of the reflectivity in each of two layers above the melting layer. In these layers above the melting layer, it is necessary to invoke assumptions of horizontal homogeneity in the shape of the profile. Simple parametrizations are used for low-level orographic growth and for the bright band, and the profile is diagnosed with the help of non-radar information. The difference between the idealized and observed profiles is expressed as a single value for an entire radar-image; the difference is minimized by iteration and this avoids using complicated methods of inversion. A simulation experiment was carried out for 15 different cases; in most of them, the incorporation of data from several elevation angles reduced bias errors at long range.The new method was then used on real radar-data. In typical frontal rainfall, it showed no consistent improvement. Because it avoids using corrections which can otherwise become detrimental at long ranges, however, the new method gave improved results when reflectivity profiles were atypical.Unresolved spatial variability of the reflectivity profile continues to be a problem.

show abstract

The little tea book / compiled by Arthur Gray ; illustrated by George W. Hood

Cited by 9 publications

References 0 publications

Determination of the Primary Structure of a Mouse γG2a Immunoglobulin Identification of the Disulfide Bridges

Determination of the Primary Structure of a Mouse γG2a Immunoglobulin Identification of the Disulfide Bridges

Determination of the Primary Structure of a Mouse IgG2a Immunoglobulin

Towards improved radar estimates of surface precipitation rate at long range

Contact Info

Product

Resources

About