The number of therapeutic monoclonal antibodies used in clinical trials has recently increased dramatically, leading to the development of optimized downstream purification processes[1]. Staphylococcal protein A （SPA...The number of therapeutic monoclonal antibodies used in clinical trials has recently increased dramatically, leading to the development of optimized downstream purification processes[1]. Staphylococcal protein A （SPA）, a cell-wall protein of Staphylococcus aureus, has been developed as a universal ligand for immunoglobulin G （IgG） purification because it binds specifically to the Fc portion of the IgG molecule of many mammals[2]. However, certain characteristics of SPA severely restrict the advancement of the antibody industry.展开更多
目的:探讨结直肠癌(colorectal cancer,CRC)中非染色体结构维持蛋白凝缩蛋白复合体I亚单位H(non-SMC condensin I complex subunit H,NCAPH)、G补缀FHA域血管新生因子1(angiogenic factor with G and FHA domains 1,AGGF1)及跨膜4L六家...目的:探讨结直肠癌(colorectal cancer,CRC)中非染色体结构维持蛋白凝缩蛋白复合体I亚单位H(non-SMC condensin I complex subunit H,NCAPH)、G补缀FHA域血管新生因子1(angiogenic factor with G and FHA domains 1,AGGF1)及跨膜4L六家族成员1(transmembrane-4-L-six-family-1,TM4SF1)蛋白质表达之间的关系及临床意义。方法:收集145例CRC术后标本和30例癌旁正常黏膜组织标本,采用免疫组织化学法检测CRC和癌旁正常黏膜组织中NCAPH、AGGF1及TM4SF1蛋白质的表达情况,分析其表达与各种临床病理因素的关系以及三者之间的相关性。结果:在CRC和癌旁组织中,NCAPH、AGGF1及TM4SF1的阳性表达率分别为55.2%、53.1%、60.7%和3.3%、6.6%、0,差异均有统计学意义(均P<0.001)。3种蛋白质的表达均与CRC的组织学分化和TNM分期有关(均P<0.001);NCAPH和TM4SF1的表达均与CRC的淋巴结转移有关(均P<0.05);NCAPH和AGGF1的表达均与CRC组织脉管侵犯有关(均P<0.05);AGGF1和TM4SF1的表达均与CRC的肿瘤浸润深度有关(均P<0.01)。TM4SF1的表达分别与NCAPH和AGGF1的表达呈正相关(r值分别为0.311和0.517,均P<0.001);同时,AGGF1与NCAPH的表达亦呈正相关(r=0.291,P=0.001)。Kaplan-Meier生存分析表明:NCAPH、AGGF1及TM4SF1的表达上调均与患者的生存率有关,NCAPH、AGGF1及TM4SF1阳性的患者生存率明显低于三者阴性患者(均P<0.05)。多因素分析表明:TNM分期、NCAPH、AGGF1及TM4SF1的表达和肿瘤脉管侵犯均是影响CRC根治术后患者预后的独立因素(均P<0.05)。结论:CRC组织中NCAPH、AGGF1及TM4SF1的表达上调与CRC的分化程度、转移和预后等因素相关,这些指标的联合检测可能作为判断CRC进展及患者预后的重要指标。展开更多
The gene fragment (191 bp) encoding protein G IgG Fc binding domain was isolated by PCR from group G streptococcus (CMCC32138), and a clone containing this gene fragment was found to give fine reactivity to human IgG ...The gene fragment (191 bp) encoding protein G IgG Fc binding domain was isolated by PCR from group G streptococcus (CMCC32138), and a clone containing this gene fragment was found to give fine reactivity to human IgG when expressed in Escherichia coli. The complete nucleotide sequence of the gene fragment was determined. One base pair differs from previously reported protein Gnucleotide sequences, and resultsin an amino acid change (Ala-Thr), but this variation makes no difference in binding to the IgG Fc part by ELISA.The secondary structure of the protein G IgG Fc binding domain has been estimated by circular dichroism and assigned by computer algorithm.It shows a typical α-helix region in this domain.By breaking this α-helix region with recombinant DNA techniques, a 44 peptide, which contained the N-terminal 27 amino acid residues of this domain, was expressed in E. coli and showed no reactivity to IgG.The hydropathicity of this domain was also analyzed and compared with that of protein A relevant domain. Some similarity was found. These results suggest that the binding mechanism of protein G to the IgG Fc part depends on hydrophobic action which comes from the α-helix in protein G molecule, just as protein A binding to IgG Fc part.展开更多
The existence of the pullback attractor for the 2D non-autonomous g-Navier- Stokes equations on some bounded domains is investigated under the general assumptions of pullback asymptotic compactness. A new method to pr...The existence of the pullback attractor for the 2D non-autonomous g-Navier- Stokes equations on some bounded domains is investigated under the general assumptions of pullback asymptotic compactness. A new method to prove the existence of the pullback attractor for the 2D g-Navier-Stokes eauations is given.展开更多
Aggrecan is the major proteoglycan in the articular cartilage. This molecule is important in the proper functioning of articular cartilage because it provides a hydrated gel structure (via its interaction with hyaluro...Aggrecan is the major proteoglycan in the articular cartilage. This molecule is important in the proper functioning of articular cartilage because it provides a hydrated gel structure (via its interaction with hyaluronan and link protein) that endows the cartilage with load-bearing properties. It is also crucial in chondroskeletal morphogenesis during development. Aggrecan is a multimodular molecule expressed by chondrocytes. Its core protein is composed of three globular domains (G1, G2, and G3) and a large extended region (CS) between G2 and G3 for glycosaminoglycan chain attachment. G1 comprises the amino terminus of the core protein. This domain has the same structural motif as link protein. Functionally, the G1 domain interacts with hyaluronan acid and link protein, forming stable ternary complexes in the extracellular matrix. G2 is homologous to the tandem repeats of G1 and of link protein and is involved in product processing. G3 makes up the carboxyl terminus of the core protein. It enhances glycosaminoglycan modification and product secretion. Aggrecan plays an important role in mediating chondrocyte-chondrocyte and chondrocyte-matrix interactions through its ability to bind hyaluronan.展开更多
基金supported by grants from the National High Technology Research and Development Program of China(863 Program)(No.2012AA020304)the National Natural Science Foundation of China(Grant No.31300643)the Innovation Fund for Postgraduate Students from the Simcere Pharmaceutical Company(No.02704051)
文摘The number of therapeutic monoclonal antibodies used in clinical trials has recently increased dramatically, leading to the development of optimized downstream purification processes[1]. Staphylococcal protein A （SPA）, a cell-wall protein of Staphylococcus aureus, has been developed as a universal ligand for immunoglobulin G （IgG） purification because it binds specifically to the Fc portion of the IgG molecule of many mammals[2]. However, certain characteristics of SPA severely restrict the advancement of the antibody industry.
文摘目的:探讨结直肠癌(colorectal cancer,CRC)中非染色体结构维持蛋白凝缩蛋白复合体I亚单位H(non-SMC condensin I complex subunit H,NCAPH)、G补缀FHA域血管新生因子1(angiogenic factor with G and FHA domains 1,AGGF1)及跨膜4L六家族成员1(transmembrane-4-L-six-family-1,TM4SF1)蛋白质表达之间的关系及临床意义。方法:收集145例CRC术后标本和30例癌旁正常黏膜组织标本,采用免疫组织化学法检测CRC和癌旁正常黏膜组织中NCAPH、AGGF1及TM4SF1蛋白质的表达情况,分析其表达与各种临床病理因素的关系以及三者之间的相关性。结果:在CRC和癌旁组织中,NCAPH、AGGF1及TM4SF1的阳性表达率分别为55.2%、53.1%、60.7%和3.3%、6.6%、0,差异均有统计学意义(均P<0.001)。3种蛋白质的表达均与CRC的组织学分化和TNM分期有关(均P<0.001);NCAPH和TM4SF1的表达均与CRC的淋巴结转移有关(均P<0.05);NCAPH和AGGF1的表达均与CRC组织脉管侵犯有关(均P<0.05);AGGF1和TM4SF1的表达均与CRC的肿瘤浸润深度有关(均P<0.01)。TM4SF1的表达分别与NCAPH和AGGF1的表达呈正相关(r值分别为0.311和0.517,均P<0.001);同时,AGGF1与NCAPH的表达亦呈正相关(r=0.291,P=0.001)。Kaplan-Meier生存分析表明:NCAPH、AGGF1及TM4SF1的表达上调均与患者的生存率有关,NCAPH、AGGF1及TM4SF1阳性的患者生存率明显低于三者阴性患者(均P<0.05)。多因素分析表明:TNM分期、NCAPH、AGGF1及TM4SF1的表达和肿瘤脉管侵犯均是影响CRC根治术后患者预后的独立因素(均P<0.05)。结论:CRC组织中NCAPH、AGGF1及TM4SF1的表达上调与CRC的分化程度、转移和预后等因素相关,这些指标的联合检测可能作为判断CRC进展及患者预后的重要指标。
文摘The gene fragment (191 bp) encoding protein G IgG Fc binding domain was isolated by PCR from group G streptococcus (CMCC32138), and a clone containing this gene fragment was found to give fine reactivity to human IgG when expressed in Escherichia coli. The complete nucleotide sequence of the gene fragment was determined. One base pair differs from previously reported protein Gnucleotide sequences, and resultsin an amino acid change (Ala-Thr), but this variation makes no difference in binding to the IgG Fc part by ELISA.The secondary structure of the protein G IgG Fc binding domain has been estimated by circular dichroism and assigned by computer algorithm.It shows a typical α-helix region in this domain.By breaking this α-helix region with recombinant DNA techniques, a 44 peptide, which contained the N-terminal 27 amino acid residues of this domain, was expressed in E. coli and showed no reactivity to IgG.The hydropathicity of this domain was also analyzed and compared with that of protein A relevant domain. Some similarity was found. These results suggest that the binding mechanism of protein G to the IgG Fc part depends on hydrophobic action which comes from the α-helix in protein G molecule, just as protein A binding to IgG Fc part.
基金Project supported by the National Natural Science Foundation of China (No. 10871156)the Fund of Xi’an Jiaotong University (No. 2009xjtujc30)
文摘The existence of the pullback attractor for the 2D non-autonomous g-Navier- Stokes equations on some bounded domains is investigated under the general assumptions of pullback asymptotic compactness. A new method to prove the existence of the pullback attractor for the 2D g-Navier-Stokes eauations is given.
文摘Aggrecan is the major proteoglycan in the articular cartilage. This molecule is important in the proper functioning of articular cartilage because it provides a hydrated gel structure (via its interaction with hyaluronan and link protein) that endows the cartilage with load-bearing properties. It is also crucial in chondroskeletal morphogenesis during development. Aggrecan is a multimodular molecule expressed by chondrocytes. Its core protein is composed of three globular domains (G1, G2, and G3) and a large extended region (CS) between G2 and G3 for glycosaminoglycan chain attachment. G1 comprises the amino terminus of the core protein. This domain has the same structural motif as link protein. Functionally, the G1 domain interacts with hyaluronan acid and link protein, forming stable ternary complexes in the extracellular matrix. G2 is homologous to the tandem repeats of G1 and of link protein and is involved in product processing. G3 makes up the carboxyl terminus of the core protein. It enhances glycosaminoglycan modification and product secretion. Aggrecan plays an important role in mediating chondrocyte-chondrocyte and chondrocyte-matrix interactions through its ability to bind hyaluronan.
