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37 results about "Water Channel Proteins" patented technology

Crystallographic structure of aquaporin 1 (AQP1) PDB 1j4n. Aquaporins, also called water channels, are integral membrane proteins from a larger family of major intrinsic proteins that form pores in the membrane of biological cells, mainly facilitating transport of water between cells.

Method for preparing vesicle with amine reaction functional groups and application of vesicle

The invention discloses a vesicle with amine reaction functional groups. The vesicle comprises ABA or AB amphiphilic block copolymers and water channel proteins. The water channel proteins are embedded in the ABA or AB amphiphilic block copolymers, and the amine reaction functional groups capable of participating in polyamide interfacial polymerization reaction are grafted on the ABA or AB amphiphilic block copolymers. The invention further provides application of the vesicle with the amine reaction functional groups to preparing a reverse osmosis membrane. The vesicle and the application havethe advantages that amine graft modification is carried out on the vesicle with the water channel proteins, accordingly, the vesicle with the water channel proteins can participate in the polyamide interfacial polymerization reaction, not only can be packaged in hyper-cross-linked structures inside polyamide, but also can be connected with the hyper-cross-linked structures inside the polyamide bychemical bonds and is stable inside the reverse osmosis membrane, the problems of translocation, deformation, rupture and the like of existing vesicles with existing water channel proteins in osmosisprocedures can be solved, and the service life of the reverse osmosis membrane with the water channel proteins can be greatly prolonged.
Owner:宁波日新恒力科技有限公司

Terahertz wave technology-based unmarked aquaporin function assessment method

ActiveCN110031423AEnables label-free evaluationEffectively reflect the degree of swellingMaterial analysis by optical meansHigh-Throughput Screening MethodsCell layer
The invention relates to a terahertz wave technology-based unmarked aquaporin function assessment method. According to the method, cells are inoculated on the surface of a constructed terahertz metamaterial chip, culture is carried out to ensure that the cells grow in an adherent state and are fused into a single-cell layer, and a terahertz time-domain spectrograph is adopted to measure the harmonic peak condition of a cell layer in isotonic buffer solution; and hypotonic buffer solution is changed, and a large number of water molecules enter the cells through aquaporins to ensure that the volumes of the initial cells are increased so as to form swelled cells. According to the method, the terahertz time-domain spectrograph is adopted to obtain the harmonic peak change condition of the adherent cell layer during osmotic pressure change, so that the cell swelling degree is effectively reflected, namely, the osmosis condition of the water molecules passing through the cell layer; and thereciprocal of a time required for achieving a maximum response value is solved according to a real-time response curve, so that the unmarked assessment of the cell aquaporin function condition can berealized. The method can be used for high-throughput screening of correlated targeted AQP drugs.
Owner:THE FIRST AFFILIATED HOSPITAL OF ARMY MEDICAL UNIV

Establishing method of high-casein ration-induced type post-weaning piglet nutritional diarrhea model

The invention relates to a post-weaning piglet nutritional diarrhea model, specifically relates to the high-casein ration-induced type post-weaning piglet nutritional diarrhea model, and belongs to the field of establishment of animal models. A establishing method of the high-casein ration-induced type post-weaning piglet nutritional diarrhea model is characterized in that a 21-day post-weaning piglet is continuously fed for a high-casein ration for 15 days, casein in the high-casein ration is a unique source of protein, the adding amount of the casein is 33.72%, and the content of crude protein in the ration is 30%; and after a test is finished, a piglet diarrhea index, a serum biochemical index, an intestinal structure form and the expression amounts of an intestinal water channel protein marker molecule and a tight junction protein marker molecule in the piglet are measured. The establishing method involved in the invention has the beneficial effects that the casein is used as the unique source of the protein, the adding amount of the casein in the ration is determined, and the high-casein ration-induced type post-weaning piglet nutritional diarrhea model is established, so thata reliable model is provided for the deep exploration and prevention of post-weaning diarrhea of newborn animals.
Owner:INST OF SUBTROPICAL AGRI CHINESE ACAD OF SCI

Screening method of banana aquaporin gene promoter transcription factor

The invention discloses a screening method of a banana aquaporin gene promoter transcription factor. The screening method includes the following steps: a core region of a promoter is judged, wherein according to a banana A genome, primers of the promoter are designed and amplified, the amplification length is 1362 bp, through plantcare and PLACE, cis-acting elements of the promoter are analyzed, GUS activity of the promoter is detected, and through dyeing conditions, the core region B of the promoter is judged; and yeast one-hybrid is conducted to screen the transcription factor interacting with the promoter, wherein the yeast one-hybrid method is used for verification, the core region B of the promoter serves as a bait section for building a bait carrier, and a banana one-hybrid library obtained through yeast drought treatment is screened. By adopting the screening method of the banana aquaporin gene promoter transcription factor, the transcription factor which is directly bonded to the MaPIP1;1 promoter under drought stress conditions is identified, therefore, research for banana aquaporin genes is more convenient, the draught resistance capability of transgenic bananas can be improved, and a draught resistance mechanism of MaPIP1;1 can be further understood.
Owner:HAIKOU EXPERIMENTAL STATION CHINESE ACAD OF TROPICAL AGRI SCI +1
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