ELUTION OF HUMAN-IGG FROM AFFINITY COLUMNS CONTAINING IMMOBILIZED VARIANTS OF PROTEIN-A

被引：19

作者：

BOTTOMLEY, SP

SUTTON, BJ

GORE, MG

机构：

[1] UNIV SOUTHAMPTON,INST BIOMOLEC SCI,DEPT BIOCHEM,SOUTHAMPTON SO16 7PX,HANTS,ENGLAND

[2] UNIV LONDON KINGS COLL,RANDALL INST,DIV BIOMED SCI,LONDON WC2B 5RL,ENGLAND

来源：

JOURNAL OF IMMUNOLOGICAL METHODS | 1995年 / 182卷 / 02期

关键词：

CHROMATOGRAPHY; AFFINITY; IGG; IMMUNOGLOBULIN BINDING; PROTEIN A;

D O I：

10.1016/0022-1759(95)00049-G

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Immobilised analogues of protein A have been used for affinity chromatographic separation of human IgG. Truncation of the C-terminal region of an engineered IgG-binding domain based upon the B domain from protein A, in combination with site-directed mutagenesis, has led to the generation of a number of proteins with a decreased affinity for IgG. The elution of human IgG from these proteins when immobilised onto a solid support occurs over the pH range 3.2-5.0 with 0.5 M acetate buffer. These proteins may be effective alternatives to standard protein A columns when milder elution conditions are required.

引用

页码：185 / 192

页数：8

共 21 条

[1] Bottomley, Popplewell, Gore, Scawen, Wan, Sutton, The stability and unfolding of an IgG-binding protein based upon the B-domain of protein A from staphylococcus aureus probed by tryptophan substitutions and fluorescence spectroscopy, Protein Eng., 7, pp. 1463-1470, (1994)
[2] Bywater, Chromatography of synthetic and biological polymers, (1978)
[3] Cedergren, Andersson, Jansson, Uhlen, Nilsson, Mutational analysis of the interaction between staphylococcal protein A and human IgG1, Protein Eng., 6, pp. 441-448, (1993)
[4] Deisenhofer, Crystallographic refinement and atomic models of a human Fc and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-A resolution, Biochemistry, 20, pp. 2361-2370, (1981)
[5] Gore, Ferris, Popplewell, Scawen, Atkinson, pH sensitive interactions between IgG and a mutated IgG-binding protein based upon two B domains of protein A from Staphylococcus aureus, Protein Eng., 5, pp. 577-582, (1992)
[6] Gouda, Torigoe, Saito, Sato, Arata, Shimada, Three dimensional solution structure of the B domain of staphylococcal protein A: comparisons of the solution and crystal structures, Biochemistry, 31, pp. 9665-9672, (1992)
[7] Hillson, Karr, Oppliger, Mannik, Sasso, The structural basis of germline-encoded V<sub>H</sub>3 immunoglobulin binding to staphylococcal protein A, J. Exp. Med., 178, pp. 331-336, (1993)
[8] Hjelm, Hjelm, Sjoquist, Protein A from Staphylococcus aureus. Its isolation by affinity chromatography and its use as an immunosorbant for isolation of immunoglobulins, FEBS Lett., 28, pp. 73-76, (1972)
[9] Huston, Cohen, Maratea, Fields, Tai, Cabral-Denison, Juffras, Rueger, Ridge, Oppermann, Keck, Multisite association by recombinant proteins can enhance binding selectivity, Biophys. J., 62, pp. 87-91, (1992)
[10] Kato, Gouda, Takaha, Yoshino, Matsunaga, Arata, <sup>13</sup>C NMR study of the mode of interaction in solution of the B fragment of staphylococcal protein A and the Fc fragments of mouse immunoglobulin G, FEBS Lett., 328, pp. 49-54, (1993)

← 1 2 3 →