Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Gisèle Préaux"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1545:104-113
A proteinase inhibitor with M(r) 697000 and 20.3% (w/w) carbohydrate was isolated from the haemolymph of the snail Helix pomatia and characterized. It was shown to have a tetrameric structure with subunits disulphide linked by two. It inhibited the a
Autor:
Jean Marie Ruysschaert, Alain Poncin, Alain Lamproye, Gisèle Préaux, Erik Goormaghtigh, Ruben Abagyan, Benoît Moreau, Joseph Martial, Annick Houbrechts, Véronique Mainfroid, Karine Goraj
Publikováno v:
"Protein Engineering, Design and Selection". 8:249-259
The sequence of octarellin I, the first de novo (beta/alpha)8 polypeptide, was revised according to several criteria, among others the symmetry of the sequence, beta-residue volume and hydrophobicity, and charge distribution. These considerations and
Autor:
Constant Gielens, Bart Devreese, Gisèle Préaux, Natalie De Geest, Xue-Qin Xin, Jozef Van Beeumen
Publikováno v:
European journal of biochemistry. 248(3)
In functional units d and g from the βc-haemocyanin of the gastropod Helix pomatia, amino acid analysis in the presence of dimethyl sulfoxide showed the occurrence of seven cysteine residues. Titration with 5,5′-dithiobis(2-nitrobenzoic acid), how
Publikováno v:
Micron. 35:99-100
Glycopeptides were isolated from functional units of two molluscan hemocyanins (Hcs). They were analyzed and localized in the sequences. A comparison with potential N-glycosylation sites of two other molluscan Hcs was made. An immunological cross-rea
Publikováno v:
Micron. 35:91-92
Autor:
W. Herreman, Gisèle Préaux, Ignace Hanssens, Frans Van Cauwelaert, Constant Gielens, Hugo Dangreau, Jean-Claude van Ceunebroeck
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 728:293-304
We investigated the interaction between alpha-lactalbumin and sonicated dimyristoylphosphatidylcholine at pH 4 and different temperatures. (1) At 23 degrees C and lipid-to-protein molar ratios below 170, the interaction results in a disruption of the
Publikováno v:
European Journal of Biochemistry. 60:271-280
A limited trypsinolysis of the tenths of beta-haemocyanin of Helix pomatia was performed at pH 8.2. The absorbance at 346 nm remained constant, indicating a preservation of the oxygen-binding sites. The five tryptic fragments were separated by chroma
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 69:455-462
1. 1. Chromatography on agarose gels at pH 5.5 in the presence of 1 M NaCI allowed to separate the total β-haemocyanin(β-Hc) of Helix pomatia from the α-haemocyanin (α-Hc). 2. 2. When crystalline β-Hc (β c -Hc) was first insolubilized by dialys
Autor:
Frans Van Cauwelaert, Hans Pottel, Jean-Claude van Ceuncbroeck, Ignace Hanssens, Gisèle Préaux
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 817:154-164
α-Lactalbumin is a globular protein containing helical regions with highly amphiphathic character. In this work, the interaction between bovine α-lactalbumin and sonicated dimyristoylphosphatidylcholine vesicles has been compared in different circu
Publikováno v:
Hoppe-Seyler´s Zeitschrift für physiologische Chemie. 360:1595-1604
The isolation of beta-lactoglobulin from milk of the goat is described. The purified protein was checked for purity and has been characterized by its gross composition and end groups. The native or the modified protein was then degraded by tryptic an