Zhou Yc

Hangzhou Medical College

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Wu Xf

Leibniz Institute for Catalysis

Cai Ym

Institute of Haematology and Blood Transfusion

YM Jin

Shanghai Veterinary Research Institute

HM Jiao

Center for Excellence in Molecular Cell Science

Yang Jh

Fujian Medical University

Liu Jw

Chinese Academy of Sciences

Pan Huang

Southwest Hospital

Yang Yz

Shenzhen Chronic Disease Prevention Center

Yongting Yu

Chinese Academy of Agricultural Sciences

Dongying Wang

Zhejiang Chinese Medical University

Cooperative Institutions

Chinese Academy of Medical Sciences & Peking Union Medical College

Chinese Academy of Sciences

Sun Yat-sen University

Institute of Zoology

University of Chinese Academy of Sciences

Tongji University

Taipei Veterans General Hospital

Soochow University

Zhejiang University

Center for Excellence in Molecular Cell Science

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[Cloning and expression of 21.7 kD protein gene of Schistosoma japonicum (Chinese strain)].

PubMed (2002)

YM Jin Lin Jj L Zhang Fu Zq Wu Xf

A 558 bp cDNA fragment was amplified by RT-PCR from adult Schistosoma japonicum(Chinese strain) mRNA with a pair of primers that were designed according to published Sj21.7p gene encoding 21.7 kD protein of Schistosoma japonicum(Philippines strain). Sequence analysis indicated that this frame, named Sj21.7 (Ch), with 99% homology to Sj21.7 p, contained a complete open reading fragment (ORF) of 21.7 kD protein gene of Schistosoma japonicum(Chinese strain). The amino acid sequence shared 98% homology with 21.7 kD protein of Schistosoma japonicum. This fragment was cloned into the expression vector pET28a (+) and subsequently expressed in Escherichia coli with IPTG induction. SDS-PAGE analysis revealed that the molecular weight of this expressed product was 25.4 kD. Western blotting showed that the recombinant protein reacted well with the rabbit serum immunized with Sj worm antigen, indicating that this expressed product had good antigenicity.

Homology

Antigenicity

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Purification, cDNA cloning and molecular characteristic of a fibrinolytic enzyme from the venom of Agkistrodon acutus.

PubMed (1998)

Du Xy Pan Huang Jin Y Hong Zhu Wu Xf

A nonglycoprotein-like fibrinolytic enzyme ((FIB-I) was purified from the crude venom of Agkistrodon acutus by CM-Sepharose CL-6B and DEAE-Sepharose CL-6B ion exchange chromatography and then by FPLC through Superose 12 gel filtration. Its molecular weight is about 23 kDa and isoelectric point is near 6.0. It not only has fibrinolytic and caseinolytic activity, but also can hydrolyze BAEE. The local hemorrhagic activity was found in mice after the subcutaneous injection of this enzyme. EDTA can inhibit its fibrinolytic activity completely, but PMSF and arrowhead proteinase inhibitor have no such obvious inhibitory effect, thus implying that FIB-I is a metalloproteinase. The N-terminal ten amino acid residues 'STEFQRYMEI' of FIB-I was elucidated. A full-length cDNA gene of this enzyme was cloned by using RT-PCR from the total RNA extracted from the snake venom gland and FIB-I was expressed in E. coli. Having analyzed the sequence, we found that it had a typical zinc-chelating characteristic as 'HEXXHXXGXXHD.'

Sepharose

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Citations (5)

Nutrient Loading of Developing Seeds

Zhang Wh Zhou Yc Dibley Ke Tyerman Sd Furbank Rt

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Citations (96)

Ipriflavone promotes osteogenesis of MSCs derived from osteoporotic rats.

PubMed (2018)

Gao Ag Zhou Yc Hu Zj BB Lu

To explore whether Ipriflavone could prevent postmenopausal osteoporosis (PMOP) and improve bone quality via promoting osteogenesis of bone marrow-derived mesenchymal stem cell (MSCs).MSCs were extracted from rats and identified using flow cytometry. Osteogenic specific genes and adipogenic specific genes in MSCs were detected by quantitative Real-time polymerase chain reaction (qRT-PCR). The effect of Ipriflavone on osteogenesis was detected by CCK-8 (cell counting kit-8) assay, ALP activity detection, alizarin red staining and Western blot, respectively. Furthermore, ovariectomized PMOP rat model was constructed. The effects of Ipriflavone on osteogenesis, BMD and bone biomechanical properties of ovariectomized rats were detected.MSCs derived from ovariectomized rats exerted multiple differentiation potentials. CCK-8 assay indicated that 0.8 μM Ipriflavone were the maximal dose that did not affect MSCs proliferation, which was selected for the following experiments. In vitro researches demonstrated that Ipriflavone remarkably promoted MSCs osteogenesis. In vivo results indicated that BMD, BV/TV, Tb.N and Tb.Th were decreased in ovariectomized rats than those of rats in sham group. Ipriflavone treatment remarkably prevented osteoporosis via promoting MSCs osteogenesis in ovariectomized rats.Ipriflavone prevents postmenopausal osteoporosis, improves bone quality and protects bone tissue via promoting MSCs osteogenesis.

10.26355/eurrev_201807_15527

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Citations (9)

Analysis of differently expressed membrane proteins between male and female worm of schistosoma japonicum after pairing

Cheng Gf JJ Lin ZQ Fu Zhou Yc Cai Ym

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[Contraception by inhibitors of acrosomal proteinase].

PubMed (1986)

Zhou Yc

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Corrigendum to “Mutations and clinical significance of calcium voltage-gated channel subunit alpha 1E (CACNA1E) in non-small cell lung cancer” [Cell Calcium 102 (2022) 102527]

Cell Calcium (2024)

Sh. Gao GZ Wang Liping Wang Lin Feng Zhou Yc

Alpha (finance)

10.1016/j.ceca.2024.102866

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Inelastic scattering in a one-dimensional mesoscopic ring at finite temperature

Helvetica physica acta (1998)

XE Yang Liyuan Zhang Zhou Yc Liu H

The effect of Mn on structure and magnetic properties of Tb2Fe17-xMnx compounds has been investigated. Substitution of Mn for Fe does not change the structure of Tb2Fe17. All compounds crystallize in the Th2Ni17-type structure. The Curie temperature of Tb2Fe17-xMnx compounds decreases monotonically with increasing Mn content. The saturated magnetic moment and the magnetic moment of the transition metal sublattice of the Tb2Fe17-xMnx compounds decrease with increasing Mn concentration. A point without zero moment similar to the compensation point was observed in the temperature dependence of magnetization for the Tb2Fe17-xMnx compound with x = 4.0, which is explained by a three-sublattice model. (C) 1998 American Institute of Physics. [S0021-8979(98)04823-3].

Mesoscopic physics

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[The hemolytic site of the basic phospholipase A(2) from Agkistrodon halys pallas].

PubMed (2002)

HM Jiao Qu Jin JJ Zhao Bo Feng Wu Xf

The gene of the basic phospholipase A(2) from Agkistrodon halys Pallas (BPLA(2) )was mutated site-directedly by polymerase chain reaction (PCR) and the residue Arg(34) of the encloding protein was substituted by Glu and Gln respectively. The mutant gene has been cloned into the expression vector pBLMVL2 and has been expressed in E.coli RR1 effectively. The protein was produced as insoluble inclusion bodies. After partial purification, the inclusion bodies were denatured and renatured into active form, and the renatured recombinant protein was purified by gel-filtration. The expression product has the same enzymatic activity as the denatured-refolded BPLA(2) and its hemolytic activity dropped distinctly, which suggest that the basic residue Arg(34) of BPLA(2) is a crucial amino acid residue during the process of hemolysis.

Inclusion bodies

Residue (chemistry)

Phospholipase A

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Citations (2)

Expression of the APLA(2) Gene from Agkistrodon halys Pallas.

PubMed (1998)

Liu Xl Pan H Yang Gz Wu Xf Zhou Yc

The APLA(2) gene from Agkistrodon halys Pallas has been cloned into the expression plasmid pBLMVL2 and expressed in E. coli RR1. The molecular weight of the expressed product is approximately 14 kD as shown by SDS-PAGE, its expression level is about 30% of the total cellular proteins. The protein was produced as insoluble inclusion bodies. After partially purified by washing the inclusion bodies, the product was denatured and refolded into active form. Then, the expressed APLA(2) was purified by FPLC Superose (TM) 12 and was a single band as shown by SDS-PAGE. The purified expressed protein had specific activity as the native enzyme and cross-reacted with antisera prepared against the native enzyme. The successful expression of the APLA(2) gene from Agkistrodon halys Pallas provides a good basis for further structure-function studies.

Inclusion bodies

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Citations (1)