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Biosynthesis, cDNA and amino acid sequences of a precursor of conglutin δ, a sulphur-rich protein from Lupinus angustifolius (1990)

Gayler, Kenwyn R. ; Kolivas, Sotirios ; Macfarlane, Alison J. ; [et al.]

Springer

Plant molecular biology 15 (1990), S. 879-893

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ISSN: 1573-5028

Keywords: Biosynthesis ; DNA sequence ; Lupinus angustifolius ; protein sequence ; plant cDNA ; 2S storage protein

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The biosynthesis of conglutin δ has been studied in developing cotyledons of Lupinus angustifolius L. Precursors of conglutin δ formed the major sink for [35S]-cysteine incorporated by developing lupin cotyledons, and these precursors were rapidly sequestered into the endoplasmic reticulum. The sequence of a cDNA clone coding for one such precursor of conglutin δ was determined. The structure of the precursor polypeptide for conglutin δ predicted from the cDNA sequence contained an N-terminal leader peptide of 22 amino acids directly preceding a subunit polypeptide of M r 4520, together with a linking region of 13 amino acids and a subunit polypeptide of M r 9558 at the C-terminus. The amino acid sequence predicted from the cDNA sequence showed minor variations from that established by sequencing of the protein purified from mature dried seeds (Lilley and Inglis, 1986). These were consistent with the existence of a multi-gene family coding for conglutin δ. Comparison of the sequences of conglutin δ with those of other 2S storage proteins showed that the cysteines involved in internal disulphide bridges between the mature subunits of conglutin δ, were maintained throughout this family of proteins but that little else was conserved either at the protein or DNA level.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00039427

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Recombinant antineuraminidase single chain antibody: Expression, characterization, and crystallization in complex with antigen (1993)

Malby, Robyn L. ; Caldwell, J. Bruce ; Gruen, L. Clem ; [et al.]

New York, NY : Wiley-Blackwell

Proteins: Structure, Function, and Genetics 16 (1993), S. 57-63

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ISSN: 0887-3585

Keywords: X-ray crystallography ; antibody domain ; recombinant DNA ; binding affinity ; antigen-antibody complex ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: The variable heavy (VH) and variable light (VL) genes of NC10, a monoclonal antibody with specificity toward N9 neuraminidase (NA), were cloned and sequenced. A single chain Fv (scFv) fragment of NC10, consisting of VH and VL domains joined by a peptide linker, was designed, constructed and expressed in the E. coli expression vector pPOW. The N-terminal secretion signal PelB directed the synthesized protein into the periplasm where it was associated with the insoluble membrane fraction. An octapeptide (FLAG) tail was fused to the C-terminus of the single chain Fv to aid in its detection and remained intact throughout the protein purification process. NC10 scFv was purified by solubilization of the E. coli membrane fraction with guanidinium hydrochloride followed by column chromatography. The purified NC10 scFv showed binding affinity for its antigen, NA, 2-fold lower than that of the parent Fab. The complex between NA and the scFv has been crystallized by the vapor diffusion method. The crystals are tetragonal, space group P4212, with unit cell dimensions a = b = 141 Å, c = 218 Å. © 1993 Wiley-Liss, Inc.

Additional Material: 4 Ill.