Affinity and hydrophobic interactions of penicillin amidase.
Hindustan Antibiot Bull
;
1989 Feb-May; 31(1-2): 25-8
Article
in English
| IMSEAR
| ID: sea-2593
ABSTRACT
Binding of penicillin amidase from E. coli 436 to aniline-, benzylamine- and phenylethylamine-Sepharose was studied. Binding of the enzyme to aniline-Sepharose was exclusively due to hydrophobic interactions. Benzylamine-Sepharose binds the enzyme due to affinity interactions in the absence of ammonium sulphate and due to hydrophobic interactions in the presence of ammonium sulphate. A conformational change in the penicillin amidase molecule due to ammonium sulphate there by exposing the side chain binding site as a hydrophobic core is suggested.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Penicillin Amidase
/
Phenethylamines
/
Benzylamines
/
Chromatography, Affinity
/
Amidohydrolases
/
Aniline Compounds
Language:
English
Journal:
Hindustan Antibiot Bull
Year:
1989
Type:
Article
Similar
MEDLINE
...
LILACS
LIS