Association of the P64k dihydrolipoamide dehydrogenase to the Neisseria meningitidis membrane
Bacterial dihydrolipoamide dehydrogenases are usually found to be part of the cytoplasmic alpha -oxoacid dehydrogenase multienzyme complexes. However, our group has been able to isolate a dihydrolipoamide dehydrogenase from Neisseria meningitidis, termed P64k, by using polyclonal antisera raised aga...
Saved in:
Published in | Biotecnología aplicada Vol. 21; no. 3; pp. 137 - 142 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
01.09.2004
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | Bacterial dihydrolipoamide dehydrogenases are usually found to be part of the cytoplasmic alpha -oxoacid dehydrogenase multienzyme complexes. However, our group has been able to isolate a dihydrolipoamide dehydrogenase from Neisseria meningitidis, termed P64k, by using polyclonal antisera raised against meningococcal outer membrane proteins. To better understand its biochemical role, protease accessibility, as well as immunoelectromicroscopy techniques were used to study the subcellular localization of P64k. Our results suggest that a significant fraction of the neisserial P64k dihydrolipoamide dehydrogenase is envelope-associated in a compartment sensitive to external proteases, although the low resolution of the methods used so far precludes a more detailed assignment of its location. |
---|---|
Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0864-4551 |