STRUCTURAL CHARACTERISTICS OF A GLOBULAR PROTEIN INVESTIGATED BY X-RAY PHOTOELECTRON-SPECTROSCOPY - COMPARISON BETWEEN A LEGUMIN FILM AND A POWDERED LEGUMIN

被引：36

作者：

LEBUGLE, A ^{[1
]}

SUBIRADE, M ^{[1
]}

GUEGUEN, J ^{[1
]}

机构：

[1] INRA,BIOCHIM & TECHNOL PROT LAB,F-44026 NANTES 03,FRANCE

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1995年 / 1248卷 / 02期

关键词：

LANGMUIR-BLODGETT FILM; LEGUMIN; XPS; ESCA; PROTEIN ORIENTATION; (P-SATIVUM);

D O I：

10.1016/0167-4838(95)00009-J

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Films of legumin, a pea protein, were deposited onto a glass support using the Langmuir-Blodgett method, at various surface pressures. XPS study of these films shows that their thickness increases with the deposition pressure. At the pressure limits of films stability, the thickness values (respectively 73 and 110 Angstrom) are close to the protein dimensions. Layered at low pressure, the oblate protein stands up when pressure increases. Furthermore, XPS study shows that the orientation of the external flexible loops depends on the obtention conditions. Thus, in the case of Langmuir-Blodgett films, hydrophobic residues are turned towards the external surface, and the hydrophilic ones towards the glass substrate. But, in the opposite, when protein is obtained by lyophilization, the hydrophilic residues are orientated outsides. It seems possible to determine by XPS the nature of the residues which give to the protein its reactivity, since they are located at its external surface.

引用

页码：107 / 114

页数：8

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