SUBUNIT-EXCHANGE CHROMATOGRAPHY OF PROTEINS - BEHAVIOR OF ALPHA-CHYMOTRYPSIN

被引：14

作者：

ANTONINI, E

CARREA, G

CREMONESI, P

PASTA, P

ROSSIFANELLI, MR

CHIANCONE, E

机构：

[1] UNIV ROME, FAC MED, INST CHEM, CNR, CTR MOLEC BIOL, I-00100 ROME, ITALY

[2] UNIV ROME, INST BIOCHEM, I-00100 ROME, ITALY

来源：

ANALYTICAL BIOCHEMISTRY | 1979年 / 95卷 / 01期

关键词：

D O I：

10.1016/0003-2697(79)90190-8

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Protein subunits attached covalently to a solid matrix bind free subunits under conditions where an association-dissociation equilibrium exists in the soluble protein. This is the basis of a process which may be called subunit-exchange chromatography. The process, which may be applied to any self-associating protein, is exemplified here with .alpha.-chymotrypsin. The behavior of the system was studied in detail, especially with respect to the conditions of immobilization of the monomer. The potential of the method for analytical and preparative purposes is discussed.

引用

页码：89 / 96

页数：8

共 10 条

[1]

Antonini E, 1976, Methods Enzymol, V44, P538

[2]

ANTONINI E, 1975, PROTEIN LIGAND INTER, P45

[3]

AUNE KC, 1971, BIOCHEMISTRY-US, V10, P1609

[4]

AUNE KC, 1971, BIOCHEMISTRY-US, V10, P1617