A process for the determination of the content of a fusion protein in a mixture of fusion protein and proteolytic degradation product

• 1. 测量血液样品中蛋白水解级联的肽降解产物的方法 [P] . 中国专利： CN104395750B . 2017.06.30
• 2. 测量血液样品中蛋白水解级联的肽降解产物的方法 [P] . 中国专利： CN104395750A . 2015-03-04
• 3. A process for the determination of the content of a fusion protein in a mixture of fusion protein and proteolytic degradation product [P] . IE67452B1 . 1996-04-03

  机译： 确定融合蛋白和蛋白水解降解产物混合物中融合蛋白含量的方法

• 4. Method for the determination of the proportion of a fusion protein in a mixture of fusion protein and proteolytic degradation products [P] . 欧洲知识产权局专利： EP0420075B1 . 1995-05-24

  机译： 测定融合蛋白和蛋白水解降解产物混合物中融合蛋白比例的方法

• 5. Method for the determination of the proportion of a fusion protein in a mixture of fusion protein and proteolytic degradation products [P] . 欧洲知识产权局专利： EP0420075A1 . 1991-04-03

  机译： 测定融合蛋白和蛋白水解降解产物混合物中融合蛋白比例的方法

• 1. The Mechanism of Henipavirus Fusion： Examining the Relationships between the Attachment and Fusion Glycoproteins [J] . Andrew C. Hickey, Christopher C. Broder 中国病毒学：英文版 . 2009,第002期
• 2. Immunogenicity and protective efficacy of DHBV DNA vaccines expressing envelope and capsid fusion proteins in ducks delivered by attenuated Salmonella typhimurium [J] . LIU Si-yang123, JIA Ren-yong123, LI Qing-qing123, 农业科学学报：英文版 . 2018,第004期
• 3. Immunogenicity and protective efficacy of DHBV DNA vaccines expressing envelope and capsid fusion proteins in ducks delivered by attenuated Salmonella typhimurium [J] . LIU Si-yang, LIU Ma-feng, ZHAO Xin-xin, 农业科学学报（英文版） . 2018,第004期
• 4. Determination of the minimal fusion peptide of HIV, SIV and BLV fusion glycoproteins [C] . Aurelien Lorin, Benoit Charloteaux, Laurence Lins American Peptide Symposium . 2009
• 5. Investigation of the proteolytic processing of the Hendra virus fusion protein. [D] . Craft, Willie Warren, Jr. 2006
• 6. Expression of the gag-pol fusion protein of Moloney murine leukemia virus without gag protein does not induce virion formation or proteolytic processing. [O] . K M Felsenstein, S P Goff 1988
• 7. Expression of the gag-pol fusion protein of Moloney murine leukemia virus without gag protein does not induce virion formation or proteolytic processing [O] . K M Felsenstein, S P Goff 1988
• 8. Proteolytic Processing of the Protease Which Initiates Degradation of Small, Acid-Soluble Proteins during Germination of Bacillus subtilis Spores [R] . Sanchez-Salas, J. L., Setlow, P. 1993

• 1. BACKGROUND： Vibrio vulnifi cus inside the body could activate the NF-!B signaling pathwayand initiate the inflammatory cascade. The lung is one of the earliest organs affected by sepsisassociated with acute lung injury. High mobility group protein B1 （HMGB1） is an important late-actingpro-infl ammatory cytokine involving in the pathophysiology of sepsis. It is also involved in the injuryprocess in the lung, liver and intestine. There has been no report on the involvement of HMGB1 inVibrio vulnifi cus sepsis-induced lung injury.METHODS： Sixty rats were randomly divided into a normal control group （group A, n=10） anda Vibrio vulnificus sepsis group （group B, n=50）. Sepsis was induced in the rats by subcutaneousinjection of Vibrio vulnificus （concentration 6×108 cfu/mL, volume 0.1 mL/100g）） into the left lowerlimbs. The rats in group B were sacrifi ced separately 1, 6, 12, 24, and 48 hours after the infection.Their lungs were stored as specimens, lung water content was measured, and lung pathology wasobserved under a light microscope. The expressions of the HMGB1 gene and protein in the lungswere detected by RT-PCR and Western blot. Data were analyzed with one-way analysis of variance（ANOVA） and the LSD method for pair-wise comparison between the two groups. P〈0.05 wasconsidered statistically signifi cant.RESULTS： Compared to group A （0.652±0.177）, HMGB1 mRNA expression in the lungs ofgroup B was signifi cantly higher at 0 hour （1.161±0.358, P=0.013）, 24 hours （1.679±0.235, P=0.000）,and 48 hours （1.258±0.274, P=0.004） （P〈0.05）, and peaked at 24 hours. Compared to group A（0.594±0.190）, HMGB1 protein expression at 6 hours （1.408±0.567, P=0.026） after infection wassignificantly increased （P〈0. 05）, and peaked at 24 hours （2.415±1.064, P=0.000） after infection.Compared to group A （0.699±0.054）, lung water content was significantly increased at 6 hours（0.759±0.030, P=0.001）,12 hours （0.767±0.023, P=0.000）, 24 hours （0.771±0.043, P=0.000） and 48hours （0.789±0.137, P=0.000） after infection （P〈0.05）. Compared to group A, pathological changesat 12 hours in group B indicate marked pulmonary vascular congestion, interstitial edema andinfl ammatory infi ltration. Alveolar cavity collapse and boundaries of the alveolar septum could not beclearly identifi ed.CONCLUSION： Vibrio vulnifi cus sepsis can lead to injury in rat lungs, and increased HMGB1expression in lung tissue may be one of the mechanisms for injury from Vibrio vulnifi cus sepsis. [J] . Qiao-meng Qiu ,Zhong-wang Li ,Lu-ming Tang . 世界急诊医学杂志(英文) . 2011,第4期
• 2. The Mechanism of Henipavirus Fusion: Examining the Relationships between the Attachment and Fusion Glycoproteins [J] . Andrew C. Hickey ,Christopher C. Broder . 中国病毒学 . 2009,第002期
• 3. 低pH孵放法灭活人重组肿瘤坏死因子α融合蛋白中异嗜性小鼠白血病毒的方法学研究 [C] . 马荣 . 中国中医科学院2013年博士生学术年会 . 2013
• 4. BDNF-TAT融合蛋白在大肠杆菌中的表达纯化及体外活性测定 [A] . 罗道飞 . 2011