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Wyświetlanie 1-2 z 2
Tytuł:
Preparation of a polyclonal antibody against hypericin synthase and localization of the enzyme in red-pigmented Hypericum perforatum L. plantlets
Autorzy:
Qian, Jie
Wu, Junyu
Yao, Bingbo
Lu, Yanhua
Powiązania:
https://bibliotekanauki.pl/articles/1039673.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
tissue localization
polyclonal antibody
hypericin synthase
Hypericum perforatum
hypericin
Opis:
Hypericum perforatum is well known for its antidepressant and anti-inflammatory activities, for which hypericin and its derivatives are indicated to be the most active compounds. Hypericin synthase (Hyp-1) is the only protein proven to catalyze the synthesis of hypericin. In this study, the full-length cDNA of Hyp-1 was chemically synthesized according to the Hyp-1 sequence in GenBank (accession no. AY148090) and then cloned into the plasmid pET22b. Hyp-1 was expressed in Escherichia coli BL21 (DE3) and purified with a Ni-NTA column. The purified protein was used to immunize New Zealand white rabbits, from which an antiserum was purified by protein G affinity chromatography. The polyclonal antibody against Hyp-1 provides a valuable tool for the study of hypericin biosynthesis in H. perforatum. Expression of Hyp-1 and the cellular distribution of hypericin were analyzed in different organs of red-pigmented H. perforatum plantlets. The black glands were not the only site of hypericin accumulation and the results indicated that hypericin might be synthesized in mesophyll cells or in tissues of the root and/or stem and then transported to the glands. This work provides a foundation for further investigation of the regulatory mechanism of hypericin synthesis during the development of H. perforatum.
Źródło:
Acta Biochimica Polonica; 2012, 59, 4; 639-645
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
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
    Wyświetlanie 1-2 z 2

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