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Study of the Alpha-l-Fucosidase Langmuir Monolayer at the Air-Water Interface.

Authors :
Waidely, Eric
Al-Youbi, Abdulrahman O.
Bashammakh, Abdulaziz S.
El-Shahawi, Mohammad S.
Leblanc, Roger M.
Source :
Journal of Physical Chemistry A. Dec2016, Vol. 120 Issue 50, p12843-12849. 7p.
Publication Year :
2016

Abstract

Alpha-l-fucosidase is a known biomarker for hepatocellular carcinoma that has shown great potential in diagnostics. Most of the focus for this enzyme has been on the free form found in serum; however, little is known of the properties of the minor portion of membrane-bound alpha-l-fucosidase. To better understand the properties of membrane-bound alpha-l-fucosidase, this enzyme was surveyed at the air-water interface. Alpha-l-fucosidase is able to form a stable Langmuir monolayer, which was confirmed through surface-pressure and surface-potential area isotherms, as well as infrared reflection-absorption spectroscopy (IRRAS). Furthermore, an interaction between the alpha-l-fucosidase Langmuir monolayer and a specific antibody for this enzyme, FUCA2, was observed. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
10895639
Volume :
120
Issue :
50
Database :
Academic Search Index
Journal :
Journal of Physical Chemistry A
Publication Type :
Academic Journal
Accession number :
120422006
Full Text :
https://doi.org/10.1021/acs.jpcb.6b09094