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Statements

Subject Item
n2:RIV%2F00216224%3A14310%2F02%3A00007921%21RIV08-GA0-14310___
rdf:type
skos:Concept n9:Vysledek
dcterms:description
Mouse major urinary proteins (MUPs) have been proposed to play a role in regulat ing the release and capture of pheromones. Here, we report affinity measurements of five recombinant urinary MUP isoforms (MUPs-I, II, VII, VIII, and IX) and on e recombinant nasal isoform (MUP-IV) for each of three pheromonal ligands, (+/- )-2-sec-butyl-4,5-dihydrothiazole (SBT), 6-hydroxy-6-methyl-3-heptanone (HMH), a nd (+/-)dehydro-exo-brevicomin (DHB). Dissociation constants for all MUP-pherom one pairs were determined by isothermal titration calorimetry, and data for SBT were corroborated by measurements of intrinsic protein fluorescence. We also rep ort the isolation of MUP-IV protein from mouse nasal extracts, in which MUP-IV m RNA has been observed previously. The affinity of each MUP isoform for SBT (Kd ~ 0.04 to 0.9 uM) is higher than that for DHB (Kd ~ 26 to 58 uM), which in turn is higher than that for HMH (Kd ~ 50 to 200 uM). Isoforms I, II, VIII, a nd IX show very similar affinities for each of the ligands. Mouse major urinary proteins (MUPs) have been proposed to play a role in regulat ing the release and capture of pheromones. Here, we report affinity measurements of five recombinant urinary MUP isoforms (MUPs-I, II, VII, VIII, and IX) and on e recombinant nasal isoform (MUP-IV) for each of three pheromonal ligands, (+/- )-2-sec-butyl-4,5-dihydrothiazole (SBT), 6-hydroxy-6-methyl-3-heptanone (HMH), a nd (+/-)dehydro-exo-brevicomin (DHB). Dissociation constants for all MUP-pherom one pairs were determined by isothermal titration calorimetry, and data for SBT were corroborated by measurements of intrinsic protein fluorescence. We also rep ort the isolation of MUP-IV protein from mouse nasal extracts, in which MUP-IV m RNA has been observed previously. The affinity of each MUP isoform for SBT (Kd ~ 0.04 to 0.9 uM) is higher than that for DHB (Kd ~ 26 to 58 uM), which in turn is higher than that for HMH (Kd ~ 50 to 200 uM). Isoforms I, II, VIII, a nd IX show very similar affinities for each of the ligands. Mouse major urinary proteins (MUPs) have been proposed to play a role in regulat ing the release and capture of pheromones. Here, we report affinity measurements of five recombinant urinary MUP isoforms (MUPs-I, II, VII, VIII, and IX) and on e recombinant nasal isoform (MUP-IV) for each of three pheromonal ligands, (+/- )-2-sec-butyl-4,5-dihydrothiazole (SBT), 6-hydroxy-6-methyl-3-heptanone (HMH), a nd (+/-)dehydro-exo-brevicomin (DHB). Dissociation constants for all MUP-pherom one pairs were determined by isothermal titration calorimetry, and data for SBT were corroborated by measurements of intrinsic protein fluorescence. We also rep ort the isolation of MUP-IV protein from mouse nasal extracts, in which MUP-IV m RNA has been observed previously. The affinity of each MUP isoform for SBT (Kd ~ 0.04 to 0.9 uM) is higher than that for DHB (Kd ~ 26 to 58 uM), which in turn is higher than that for HMH (Kd ~ 50 to 200 uM). Isoforms I, II, VIII, a nd IX show very similar affinities for each of the ligands.
dcterms:title
Pheromone binding by polymorphic mouse major urinary proteins Pheromone binding by polymorphic mouse major urinary proteins Pheromone binding by polymorphic mouse major urinary proteins
skos:prefLabel
Pheromone binding by polymorphic mouse major urinary proteins Pheromone binding by polymorphic mouse major urinary proteins Pheromone binding by polymorphic mouse major urinary proteins
skos:notation
RIV/00216224:14310/02:00007921!RIV08-GA0-14310___
n3:strany
2247
n3:aktivita
n13:P
n3:aktivity
P(GA203/00/0511)
n3:cisloPeriodika
11
n3:dodaniDat
n5:2008
n3:domaciTvurceVysledku
n12:4257707
n3:druhVysledku
n14:J
n3:duvernostUdaju
n7:S
n3:entitaPredkladatele
n15:predkladatel
n3:idSjednocenehoVysledku
658159
n3:idVysledku
RIV/00216224:14310/02:00007921
n3:jazykVysledku
n17:eng
n3:klicovaSlova
Binding affinity; isothermal titration calorimetry; major urinary proteins eins; pheromones; selectivity
n3:klicoveSlovo
n6:Binding%20affinity n6:isothermal%20titration%20calorimetry n6:selectivity n6:pheromones n6:major%20urinary%20proteins%20eins
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[BF1E70414CFE]
n3:nazevZdroje
Protein Science
n3:obor
n18:CE
n3:pocetDomacichTvurcuVysledku
1
n3:pocetTvurcuVysledku
5
n3:projekt
n16:GA203%2F00%2F0511
n3:rokUplatneniVysledku
n5:2002
n3:svazekPeriodika
11
n3:tvurceVysledku
Novotný, Milos V. Vaughn, Jeffrey L. Sharrow, Scott D. Stone, Martin J. Žídek, Lukáš
s:issn
0961-8368
s:numberOfPages
10
n11:organizacniJednotka
14310