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Statements

Subject Item
n2:RIV%2F67985823%3A_____%2F02%3A20030020%21RIV%2F2004%2FAV0%2FA20004%2FN
rdf:type
n3:Vysledek skos:Concept
dcterms:description
With respect to the mechanism of chaperone-like activity, we examined the behaviour of haptoglobin under heat shock conditions. Secondary structure changes during heat treatment were followed by circular dichroism, Raman spectroscopy and infrared spectroscopy. A model of the haptoglobin tetramer, based on its sequence homology with serine proteases and the CCP modules, has been proposed. Sequence regions responsible for the chaperone-like activity were not fully identical with the region that took part in formation of the hemoglobin-haptoglobin complex. We can postulate presence of at least two different chaperone-binding sites on each haptoglobin heavy chain. With respect to the mechanism of chaperone-like activity, we examined the behaviour of haptoglobin under heat shock conditions. Secondary structure changes during heat treatment were followed by circular dichroism, Raman spectroscopy and infrared spectroscopy. A model of the haptoglobin tetramer, based on its sequence homology with serine proteases and the CCP modules, has been proposed. Sequence regions responsible for the chaperone-like activity were not fully identical with the region that took part in formation of the hemoglobin-haptoglobin complex. We can postulate presence of at least two different chaperone-binding sites on each haptoglobin heavy chain.
dcterms:title
Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites. Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites.
skos:prefLabel
Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites. Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites.
skos:notation
RIV/67985823:_____/02:20030020!RIV/2004/AV0/A20004/N
n4:strany
1667;1676
n4:aktivita
n16:Z
n4:aktivity
Z(AV0Z5011922), Z(MSM 113100001)
n4:cisloPeriodika
10
n4:dodaniDat
n6:2004
n4:domaciTvurceVysledku
n9:1810561
n4:druhVysledku
n17:J
n4:duvernostUdaju
n15:S
n4:entitaPredkladatele
n10:predkladatel
n4:idSjednocenehoVysledku
665699
n4:idVysledku
RIV/67985823:_____/02:20030020
n4:jazykVysledku
n11:eng
n4:klicovaSlova
chaperone; haptoglobin; molecular modeling
n4:klicoveSlovo
n13:chaperone n13:haptoglobin n13:molecular%20modeling
n4:kodStatuVydavatele
DE - Spolková republika Německo
n4:kontrolniKodProRIV
[839934B23E81]
n4:nazevZdroje
Biological Chemistry
n4:obor
n8:BO
n4:pocetDomacichTvurcuVysledku
1
n4:pocetTvurcuVysledku
6
n4:pocetUcastnikuAkce
0
n4:pocetZahranicnichUcastnikuAkce
0
n4:rokUplatneniVysledku
n6:2002
n4:svazekPeriodika
383
n4:tvurceVysledku
Hofbauerová, Kateřina Ettrich, R. Brandt, W. Pavlíček, Z. Kopecký jr., V. Baumruk, V.
n4:zamer
n14:MSM%20113100001 n14:AV0Z5011922
s:issn
1431-6730
s:numberOfPages
10