Zobrazeno 1 - 10
of 29
pro vyhledávání: '"A. Gerbanowski"'
Publikováno v:
In Journal of Colloid And Interface Science 2003 262(2):391-399
Publikováno v:
Journal of Colloid and Interface Science. 262:391-399
The influence of grafting aliphatic or aromatic groups on the behaviors of bovine serum albumin (BSA) and rapeseed proteins (napin and cruciferin) at the air/water interface is studied. From compression isotherms, it is shown that the chemical modifi
Publikováno v:
Accreditation and Quality Assurance. 2:69-75
Method validation procedure requires a strategy for collecting those validation data that are best adapted to the analytical technique used. A flexible and general approach based on Object Linking and Embedding technology is proposed. It allows a tra
Autor:
Gerbanowski, A., Rabiller, C.
Publikováno v:
Journal of Colloid and Interface Science
Journal of Colloid and Interface Science, Elsevier, 2003, 262, pp.391-399
Journal of Colloid and Interface Science, Elsevier, 2003, 262, pp.391-399
International audience
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::18c2ad2b129c80fea9396363f083023d
https://hal.inrae.fr/hal-02672606
https://hal.inrae.fr/hal-02672606
Publikováno v:
Workshop
Workshop, Jun 2001, Nantes, France
Workshop, Jun 2001, Nantes, France
National audience
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::28930e931da1da1bbbc4df25d77b7fc2
https://hal.inrae.fr/hal-02759990
https://hal.inrae.fr/hal-02759990
Publikováno v:
Journal of agricultural and food chemistry. 47(12)
Lysyl residues of rapeseed napin (2S) and cruciferin (12S) were acylated and sulfamidated by means of anhydrides and sulfonyl chlorides, respectively. The secondary and tertiary structures as well as the surface hydrophobicity of the modified protein
Publikováno v:
Journal of Agricultural and Food Chemistry
Journal of Agricultural and Food Chemistry, American Chemical Society, 1999, 47 (12), pp.5218-5226
Journal of Agricultural and Food Chemistry, American Chemical Society, 1999, 47 (12), pp.5218-5226
International audience
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::5d2e1e0ae9ab9f750e3f9776c2f4f8db
https://hal.inrae.fr/hal-02694151
https://hal.inrae.fr/hal-02694151
Publikováno v:
Journal of Protein Chemistry
Journal of Protein Chemistry, Springer-Verlag;Springer (Kluwer Academic Publishers), 1999, 18 (3), pp.325-336. ⟨10.1023/A:1021043529923⟩
Journal of Protein Chemistry, Springer-Verlag;Springer (Kluwer Academic Publishers), 1999, 18 (3), pp.325-336. ⟨10.1023/A:1021043529923⟩
Bovine serum albumin was chosen as a model protein to study the effect of the functionalization of the epsilon-NH2 of lysine residues with different carbon chains on the physical properties of proteins. Thus, BSA has been acylated and sulfonylated by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b63f20185743d4f63f31389e8c0b789
https://hal.inrae.fr/hal-02695586
https://hal.inrae.fr/hal-02695586