Photolabeling of the alpha-neuraminidase/beta-galactosidase complex from human placenta with a photoreactive neuraminidase inhibitor

Journal Article · Fri Nov 30 04:00:00 EST 1990 · Biochemical and Biophysical Research Communications; (USA)

DOI:https://doi.org/10.1016/S0006-291X(05)81014-9· OSTI ID:6072439

Warner, T G; Louie, A; Potier, M ^[1]

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1. Univ. of Tennessee, Memphis (USA)

Photolabeling of the alpha-neuraminidase/beta-galactosidase complex in human placenta was carried out using the radioactive photoprobe, 9-S-(4-azido-3,5-3H-2-nitrophenyl)-5-acetamido-2,6 anhydro-2,3,5,9- tetradeoxy-9- thio-D-glycero-D-galacto-non-2-enonic acid. Two intensely labeled bands at 61 and 46 kD were detected with autoradiography. Labeling of the 46 kD protein was blocked with the inclusion of the surfactant Triton X-100 in the photolysis mixture, indicating a nonspecific, hydrophobic interaction. The 61 kD protein was protected from labeling only when the neuraminidase inhibitor 2,3 dehydro N-acetyl neuraminic acid (1 mM) was present during photolysis. These results suggest that the neuraminidase activity resides among the proteins in the 61 kD molecular weight range comigrating with the lysosomal beta-galactosidase, under denaturing conditions.

• OSTI ID: 6072439
• Journal Information: Biochemical and Biophysical Research Communications; (USA), Journal Name: Biochemical and Biophysical Research Communications; (USA) Vol. 173:1; ISSN BBRCA; ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AFFINITY
ANIMALS
AUTORADIOGRAPHY
COMPLEXES
ELECTROPHORESIS
ENZYME ACTIVITY
ENZYME INHIBITORS
ENZYMES
FETAL MEMBRANES
GALACTOSIDASE
GLYCOSYL HYDROLASES
HYDROGEN COMPOUNDS
HYDROLASES
LABELLING
MAMMALS
MAN
MEMBRANES
MOLECULAR WEIGHT
O-GLYCOSYL HYDROLASES
PLACENTA
PRIMATES
TRITIUM COMPOUNDS
VERTEBRATES