Expression of a lipocalin in prokaryote and eukaryote cells:: Quantification and structural characterization of recombinant bovine β-lactoglobulin

被引：21

作者：

Chatel, JM

Adel-Patient, K

Créminon, C

Wal, JM

机构：

[1] Ctr Etud Saclay, CEA, INRA, Lab Immuno Allergie Alimentaire, F-91191 Gif Sur Yvette, France

[2] Ctr Etud Saclay, CEA, Lab Etud Radioimmunol, DRM SPI, F-91191 Gif Sur Yvette, France

来源：

PROTEIN EXPRESSION AND PURIFICATION | 1999年 / 16卷 / 01期

关键词：

D O I：

10.1006/prep.1999.1055

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

In this paper we quantify and characterize the expression of recombinant beta-lactoglobulin (rBLG) in prokaryote and eukaryote cells. In Escherichia coli we used the pET26 vector, which permits the secretion of rBLG in periplasm, We studied the expression of rBLG in COS-7 cells and in vivo in mouse tibialis muscle. The expression of rBLG was measured by two immunoassays specific, respectively, for BLG in its native and denatured conformation. We observed that rBLG was essentially expressed in a denatured form in E. coli even in the periplasm, whereas rBLG in eukaryote cells was found in its native conformation. (C) 1999 Academic Press.

引用

收藏

页码：70 / 75

页数：6

相关论文

共 28 条

[11] Inhibition of specific IgE response in vivo by allergen-gene transfer [J].

Hsu, CH ;

Chua, KY ;

Tao, MH ;

Huang, SK ;

Hsieh, KH .

INTERNATIONAL IMMUNOLOGY, 1996, 8 (09) :1405-1411

[12] Immunoprophylaxis of allergen-induced immunoglobulin E synthesis and airway hyperresponsiveness in vivo by genetic immunization [J].

Hsu, CH ;

Chua, KY ;

Tao, MH ;

Lai, YL ;

Wu, HD ;

Huang, SK ;

Hsieh, KH .

NATURE MEDICINE, 1996, 2 (05) :540-544

[13] TRYPTOPHAN-19 OF BETA-LACTOGLOBULIN, THE ONLY RESIDUE COMPLETELY CONSERVED IN THE LIPOCALIN SUPERFAMILY, IS NOT ESSENTIAL FOR BINDING RETINOL, BUT RELEVANT TO STABILIZING BOUND RETINOL AND MAINTAINING ITS STRUCTURE [J].

KATAKURA, Y ;

TOTSUKA, M ;

AMETANI, A ;

KAMINOGAWA, S .

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY, 1994, 1207 (01) :58-67

[14] High-level expression of bovine β-lactoglobulin in Pichia pastoris and characterization of its physical properties [J].

Kim, TR ;

Goto, Y ;

Hirota, N ;

Kuwata, K ;

Denton, H ;

Wu, SY ;

Sawyer, L ;

Batt, CA .

PROTEIN ENGINEERING, 1997, 10 (11) :1339-1345

[15] The major dog allergens, Can f1 and Can f2, are salivary lipocalin proteins:: cloning and immunological characterization of the recombinant forms [J].

Konieczny, A ;

Morgenstern, JP ;

Bizinkauskas, CB ;

Lilley, CH ;

Brauer, AW ;

Bond, JF ;

Aalberse, RC ;

Wallner, BP ;

Kasaian, MT .

IMMUNOLOGY, 1997, 92 (04) :577-586

[16] Complementary DNA cloning of the predominant allergen of bovine dander: A new member in the lipocalin family [J].

Mantyjarvi, R ;

Parkkinen, S ;

Rytkonen, M ;

Pentikainen, J ;

Pelkonen, J ;

Rautiainen, J ;

Zeiler, T ;

Virtanen, T .

JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY, 1996, 97 (06) :1297-1303

[17] LOCATION OF SULFHYDRYL AND DISULFIDE GROUPS IN BOVINE BETA-LACTOGLOBULINS AND EFFECTS OF UREA [J].

MCKENZIE, HA ;

SHAW, DC ;

RALSTON, GB .

BIOCHEMISTRY, 1972, 11 (24) :4539-&

[18] Protein folding in the bacterial periplasm [J].

Missiakas, D ;

Raina, S .

JOURNAL OF BACTERIOLOGY, 1997, 179 (08) :2465-2471

[19] Two-site enzyme immunometric assays for determination of native and denatured β-lactoglobulin [J].

Negroni, L ;

Bernard, H ;

Clement, G ;

Chatel, JM ;

Brune, P ;

Frobert, Y ;

Wal, JM ;

Grassi, J .

JOURNAL OF IMMUNOLOGICAL METHODS, 1998, 220 (1-2) :25-37

[20] THE STRUCTURE OF BETA-LACTOGLOBULIN AND ITS SIMILARITY TO PLASMA RETINOL-BINDING PROTEIN [J].

PAPIZ, MZ ;

SAWYER, L ;

ELIOPOULOS, EE ;

NORTH, ACT ;

FINDLAY, JBC ;

SIVAPRASADARAO, R ;

JONES, TA ;

NEWCOMER, ME ;

KRAULIS, PJ .

NATURE, 1986, 324 (6095) :383-385