Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

Wyszukujesz frazę "serpin" wg kryterium: Temat


Wyświetlanie 1-3 z 3
Tytuł:
Molecular cloning, expression and characterization of Bmserpin-2 gene from Bombyx mori
Autorzy:
Pan, Ye
Xia, Hengchuan
Lü, Peng
Chen, KePing
Yao, Qin
Chen, Huiqin
Gao, Lu
He, Yuanqing
Wang, Lin
Powiązania:
https://bibliotekanauki.pl/articles/1040486.pdf
Data publikacji:
2009
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
serpin-2
Bombyx mori
bioinformatics
subcellular location
qPCR
Opis:
Serpins are a broadly distributed family of protease inhibitors. In this study, the gene encoding Bombyx mori serpin-2 (Bmserpin-2) was cloned and expressed in E. coli. The Bmserpin-2 cDNA contains a 1125 bp open reading frame (ORF). The deduced protein has 374 amino-acid residues, contains a conserved SERPIN domain and shares extensive homology with other invertebrate serpins. RT-PCR analysis showed that Bmserpin-2 was expressed in all developmental stages of B. mori larvae and various larval tissues. Subcellular localization analysis indicated that Bmserpin-2 protein was located in the cytoplasm. Interestingly, real-time quantitative PCR revealed that the expression of Bmserpin-2 in the midgut of susceptible B. mori strain 306 significantly increased at 72 hours post inoculation (hpi) when infected with BmNPV. However, there was no significant increase of the Bmserpin-2 expression in resistant strain NB infected with BmNPV. Thus, our data indicates that Bmserpin-2 may be involved in B. mori antiviral response.
Źródło:
Acta Biochimica Polonica; 2009, 56, 4; 671-677
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Origin of circulating acute phase cytokines: modified proteins may trigger il-6 production by macrophages. Preliminary report
Autorzy:
Koj, A
Guzdek, A.
Potempa, J.
Korzus, E.
Travis, J.
Powiązania:
https://bibliotekanauki.pl/articles/68989.pdf
Data publikacji:
1994
Wydawca:
Polskie Towarzystwo Fizjologiczne
Tematy:
interleukin 6
macrophage
acute phase cytokine
cytokine
modified protein
glycated albumin
fibrinogen degradation product
modified serpin
Źródło:
Journal of Physiology and Pharmacology; 1994, 45, 1
0867-5910
Pojawia się w:
Journal of Physiology and Pharmacology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Polyphenol oxidase from wheat bran is a serpin
Autorzy:
Yamasaki, Yoshiki
Konno, Haruyoshi
Noda, Kazuhiko
Powiązania:
https://bibliotekanauki.pl/articles/1040750.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
polyphenol oxidase
serpin
wheat bran
Opis:
Polyphenol oxidase (PPO; EC 1.10.3.2) was isolated from wheat bran by a procedure that included ammonium sulfate fractionation, batch adsorption by DEAE-cellulofine, CM-cellulofine column chromatography, DEAE-cellulofine column chromatography, preparative isoelectric focusing, adsorption on the membrane of a Vivapure Q Maxi H spin column, and heat treatment. These procedures led to 150-fold purification with 4.2% recovery. The PPO was homogeneous by SDS/PAGE. The relative molecular weight of the PPO was estimated to be 37000 based on its mobility in SDS/PAGE. The isoelectric point of the PPO was 4.4. The Km values of the PPO for caffeic acid, chlorogenic acid, pyrocatechol, 4-methyl catechol and l-DOPA as substrates were 0.077, 0.198, 1.176, 1.667 and 4.545 mM. The PPO was strongly inhibited by tropolone. The Ki value for tropolone is 2.2 × 10-7 M. The sequence of the 15 N-terminal amino-acid residues was determined to be ATDVRLSIAHQTRFA, which was identical to those of serpin from Triticum aestivum and protein Z from Hordeum vulgare. The PPO strongly inhibited the activity of trypsin, which is an enzyme of serine proteases; 50% inhibition was observed with 1.5 × 10-7 M PPO. The Ki value for PPO is 2.3 × 10-8 M. The wheat bran PPO should be a very important protein for protecting wheat against disease, virus, insect and herbivore damages by both the activities of PPO and protease inhibitor.
Źródło:
Acta Biochimica Polonica; 2008, 55, 2; 325-328
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

    Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies