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...

Full description

Saved in:
Bibliographic Details
Published inBiotecnología aplicada Vol. 21; no. 3; pp. 137 - 142
Main Authors Alvarez, Anabel, Martin, Alejandro, Falcon, Viviana, De la Rosa, Maria C, Gonzalez, Sonia, Guillen, Gerardo, Silva, Ricardo
Format Journal Article
LanguageEnglish
Published 01.09.2004
Subjects
Online AccessGet full text

Cover

Loading…
More Information
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