1.
J Chromatogr
; 376: 259-67, 1986 Apr 11.
Article
in English
| MEDLINE
| ID: mdl-3086352
ABSTRACT
We propose a new affinity sorbent, matrix-linked histidine, for the large-scale purification of proteins. A variety of proteins and certain peptides, each distinct from the other, were purified. Immunoglobulin G from human placenta was chosen for a detailed study concerning the effects of coupling, spacer-arm and other parameters. Multiple interactions such as charge-transfer and other ionic reactions have been suggested to be responsible for the interactions between proteins and ligand.
Subject(s)
Proteins/isolation & purification , Serine Endopeptidases , Animals , Carboxypeptidases/isolation & purification , Cathepsin A , Cattle , Chick Embryo , Chymosin/isolation & purification , Endopeptidases/isolation & purification , Female , Histidine/isolation & purification , Humans , Immunoelectrophoresis , Immunoglobulin G/isolation & purification , Peptides/isolation & purification , Placenta/analysis , Pregnancy , Saccharomyces cerevisiae/enzymology , Saccharomyces cerevisiae Proteins , Sepharose/analogs & derivatives , Sepharose/isolation & purification , Spectrophotometry, Ultraviolet
2.
J Chromatogr
; 303(1): 285-90, 1984 Oct 26.
Article
in English
| MEDLINE
| ID: mdl-6439726
