An antibody purified with a lambda GT11 fusion protein precipitates enkephalinase activity.
An antiserum was raised against the neutral endopeptidase "enkephalinase" in guinea pig and used to probe a rabbit kidney cDNA expression library. A positive clone has been isolated and sequenced. The identity of the corresponding fusion protein was ascertained by its ability to select, from the crude antiserum, antibodies which specifically immunoprecipitate neutral endopeptidase enzymatic activity. This approach eliminates the uncertainty inherent to clone identification obtained from oligonucleotide probe derived from a partial sequence of the protein.
Kahn
P H
PH
Powell
J F
JF
Beaumont
A
A
Roques
B P
BP
Mallet
J J
JJ
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D001483:Base Sequence; D003001:Cloning, Molecular; D003090:Coliphages / Q000235:genetics; D004247:DNA / Q000032:analysis; D010450:Endopeptidases / Q000235:genetics* / Q000276:immunology / Q000302:isolation & purification; D007672:Kidney Cortex / Q000201:enzymology; D015260:Neprilysin; D011817:Rabbits; D011993:Recombinant Fusion Proteins / Q000276:immunology*; D011994:Recombinant Proteins / Q000276:immunology*
D000906:Antibodies; D000936:Antigen-Antibody Complex; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D004247:DNA; D010450:Endopeptidases; D015260:Neprilysin