传统功法对新冠肺炎呼吸系统和消化系统症状的防治

新型冠状病毒肺炎呼吸道症状以干咳为主,并逐渐出现呼吸困难。六字诀属于呼吸训练法,涉及缩唇呼吸及腹式呼吸等方式,通过"嘘、呵、呼、呬、吹、嘻"六字发音协助胸腹部呼吸运动,增加呼吸道压力,促进肺部残气排出,同时提高肺部气体交换效率,改善患者呼吸功能。太极拳讲究呼吸,注重"意、气、形、神"相结合,能改善新型冠状病毒肺炎患者呼吸困难及机体缺氧状态,对咳嗽、咳痰亦有改善作用。易筋经通过伸筋、拔骨、旋转脊柱等方法,增强肢体的力量,拉伸关节、大小肌群和筋膜,利用肢体反复的伸、收、展、合、转,使胸廓充分开合,刺激呼吸肌群,增强呼吸肌肌力、耐力、伸缩性,提高呼吸肌的储备力。延年九转法以按摩为主,导引及静功为辅,重在摩腹,能通和上下,充实五脏,理气宽中、和胃降逆、有效改善消化系统症状。     

取象比类法在中药药性研究中的应用

传统取象比类法对中药药性的认识,是将中药的性能、功效与其形态、质地、颜色、气味、生长环境、入药部位、采收季节、物性等自然属性相关联,联系阴阳五行、脏腑经络、五运六气等学说,结合药物作用于人体后的反应,以推演药物的四气五味、升降浮沉、归经、毒性、功效等药性。尽管取象比类法在中药药性理论研究中与中医理论紧密相连,且对中药药性的研究逐渐成熟化,但依旧具备了主观性较强、注重特殊性和典型性而忽略普遍性等缺陷。对于取象比类法的研究需正确认识,取其精华,充分运用现代技术手段不断创新,最终构建一个传统与现代兼备的取象比类法,为现代中药药性研究提供新思路。     

不同剂量右美托咪定复合酒石酸布托啡诺在老年髋关节置换术后静脉自控镇痛中的效果

目的：探究不同剂量右美托咪定复合酒石酸布托啡诺在老年髋关节置换术后静脉自控镇痛中的效果。方法：选取2018 年6 月至2019 年6 月在河北北方学院附属第一医院择期行全髋关节置换术的患者60 例,年龄60~75 岁,随机分成三组（对照组C 组、实验组D1 组和D2 组）,每组20 例,术后均采用静脉自控镇痛（patientcontrolled intravenous analgesia,PCIA）,C 组的PCIA 泵的镇痛配方为酒石酸布托啡诺0.15 mg·kg-1;D1 组的镇痛配方为酒石酸布托啡诺0.15 mg·kg-1+ 右美托咪定1.5 μg·kg-1;D2 组的镇痛配方为酒石酸布托啡诺0.15 mg·kg-1+ 右美托咪定2.0 μg·kg-1,三组均用生理盐水稀释至100 mL,于手术结束后连接至患者,观察记录患者术后 4、8、24、36、48 h 的 VAS 评分、Ramsay 镇静评分、血压、心率、48 h 内不良反应发生情况及PCIA 有效按压次数。结果：与C 组相比,D1 组及D2 组各个时点的VAS 评分、Ramsay 镇静评分均优于C 组（P<0.05）,D1 组、D2 组患者各个时点的VAS 评分、Ramsay 评分均无明显差异（P>0.05）;与C 组相比,D1 组及D2 组患者的血流动力学指标波动程度均小于C 组,差异有统计学意义（P<0.05）;C 组患者恶心、呕吐、头晕的发生率高于D1 组和D2 组（P<0.05）,D2 组患者低血压、心动过缓的发生率明显高于C 组和D1 组（P<0.05）;D1、D2 组的PCIA 有效按压次数明显少于C 组（P<0.05）。结论：1.5 μg·kg-1 右美托咪定复合0.15 mg·kg-1 酒石酸布托啡诺应用于老年髋关节置换术后PCIA 能产生可靠的镇痛效果,降低术后不良反应的发生率。     

小儿麻醉医师迈向围术期医师理念的培养

随着现代医学的飞速发展,麻醉学正向围术期医学转变。培养小儿麻醉医师向围术期医师转变的理念,需要在了解儿童病理生理特点的前提下,重点培训小儿麻醉术前访视、术中麻醉相关技能、术后访视、围术期疼痛相关管理及心理创伤的预防与治疗。让患儿安全舒适地度过围术期、减少术后并发症及死亡率、改善远期预后,是每位小儿围术期医师的责任。     

葛类中药的品种沿革、产区及功效考证

对葛属资源记载情况进行整理和历代本草学的研究认为,南北朝以前时期用的葛根品种为野葛,南北朝至汉唐时期记载为甘葛藤,宋代及明清以后本草记载葛根品种开始多样化发展,出现家种和野生两品种并列的情况,为甘葛藤和野葛,药食两用一直沿用至今。《本草品汇精要》记载以江浙、南康、庐陵为道地,当今道地产区不明显。葛类中药古今用药功效基本一致。野葛和甘葛藤为主流品种,该属其它资源是否都能药用需进一步临床验证。《中国药典》分列葛根和粉葛两药,应以临床为导向更加完善质量标准。该研究为葛类中药的进一步鉴别研究和质量控制提供依据与参考。     

COVID-19疑似病房护理人员压力的质性研究

目的：了解COVID-19疑似病房护理人员的压力状况,为缓解临床护理人员的压力提供参照。方法：采用现象学研究法,于2020 年2月2日至2020 年3月2日,对温州医科大学附属第二医院育英儿童医院8 名COVID-19疑似病房护理人员进行半结构式访谈,运用Colaizzi七步分析法对资料进行分析。结果：对疑似病房护理人员的压力可归纳出三个主题：工作压力,社会支持利用度减少,负性情绪难以排解。其中工作压力包含3 个次主题：负荷重、社会期待高、职业暴露。结论：COVID-19疑似病房护理人员存在多方面的工作压力,应加强人力资源配置优化管理,做好COVID-19相关知识宣传,及时更新防护措施及知识,加强人文关怀,缓解护理人员压力     

2型糖尿病患者生化指标与甲状腺功能指标分析

目的探讨2型糖尿病患者生化指标与甲状腺功能指标的变化,以及2糖尿病患者甲状腺疾病的患病情况。方法随机选取2014年1月至6月我院住院的2型糖尿病患者(T2DM)295例(2型糖尿病组),健康人员80例(对照组),检测其生化指标15项:丙氨酸氨基转移酶(ALT)、天冬氨酸氨基转移酶(AST)、总蛋白(TP)、白蛋白(ALB)、碱性磷酸酶(ALP)、γ-谷氨酰基转移酶(GGT)、葡萄糖(GLU)、肌酸激酶(CK)、总胆固醇(CH)、甘油三酯(TG)、高密度脂蛋白胆固醇(HDL)、低密度脂蛋白胆固醇(LDL)、钙(Ca)、磷(P)、糖化血红蛋白(Hb A1c),甲状腺功能指标5项:甲状腺素(T4)、三碘甲腺原氨酸(T3)、游离T4(FT4)、游离T3(FT3)、促甲状腺激素(TSH),并对2型糖尿病组结合临床资料进行分析。结果2型糖尿病组中生化类指标TP、ALB、GLU、CH、TG、Ca、P、HDL、LDL、Hb A1c及甲状腺功能指标T3、FT3与对照组相比均有统计学意义(P<0.05);2型糖尿病组中患有甲状腺结节的患者比例最高,为44.7%;将2型糖尿病患者分为甲状腺结节组,其它甲状腺疾病组,甲状腺正常组,将甲状腺结节组和甲状腺正常组进行比较,年龄差异具有统计学意义(P<0.01),甲状腺结节组为53±12岁,甲状腺正常组为46±13岁,性别无差异(P>0.05),糖尿病病程差异具有统计学意义(P<0.01),甲状腺结节组为9±6年,甲状腺正常组为7±6年,对两组代谢指标进行分析,FT3差异显著(P<0.05),甲状腺结节组为4.48±0.82pmol/L,甲状腺正常组为4.67±0.67pmol/L,其它指标差异均无统计学意义(P>0.05);将2型糖尿病患者按空腹血糖水平分为A、B、C三组,血糖越高,甲状腺结节的比例越高,但差异无统计学意义(P>0.05)。结论 2型糖尿病患者其T3、FT3和一系列生化指标会发生变化,监测这些指标有助于对2型糖尿病进行更为全面的评估,且2型糖尿病患者中,甲状腺结节发病比例较高,且与年龄和病程相关,对于年龄较大和病程较长的患者更要关注甲状腺的检查。     

Capsid expansion mechanism of bacteriophage T7 revealed by multistate atomic models derived from cryo-EM reconstructions

Many dsDNA viruses first assemble a DNA-free procapsid, using a scaffolding protein-dependent process. The procapsid, then, undergoes dramatic conformational maturation while packaging DNA. For bacteriophage T7 we report the following four single-particle cryo-EM 3D reconstructions and the derived atomic models: procapsid (4.6-Å resolution), an early-stage DNA packaging intermediate (3.5 Å), a later-stage packaging intermediate (6.6 Å), and the final infectious phage (3.6 Å). In the procapsid, the N terminus of the major capsid protein, gp10, has a six-turn helix at the inner surface of the shell, where each skewed hexamer of gp10 interacts with two scaffolding proteins. With the exit of scaffolding proteins during maturation the gp10 N-terminal helix unfolds and swings through the capsid shell to the outer surface. The refolded N-terminal region has a hairpin that forms a novel noncovalent, joint-like, intercapsomeric interaction with a pocket formed during shell expansion. These large conformational changes also result in a new noncovalent, intracapsomeric topological linking. Both interactions further stabilize the capsids by interlocking all pentameric and hexameric capsomeres in both DNA packaging intermediate and phage. Although the final phage shell has nearly identical structure to the shell of the DNA-free intermediate, surprisingly we found that the icosahedral faces of the phage are slightly (∼4 Å) contracted relative to the faces of the intermediate, despite the internal pressure from the densely packaged DNA genome. These structures provide a basis for understanding the capsid maturation process during DNA packaging that is essential for large numbers of dsDNA viruses.Many dsDNA viruses, including tailed phages and herpes viruses, initially assemble a DNA-free procapsid with assistance of a network of scaffold proteins. Accompanying the exit of scaffolding proteins during subsequent ATP-driven DNA packaging, the icosahedral shell of the procapsid undergoes dramatic conformational changes and matures into a typically larger and more angular shell of the infectious phage (1–6). However, structural details, including those of capsid intermediates, are limited to the phage HK97 system (5, 7–9), for which recombinantly produced procapsid and nonphysiological conversion products were analyzed.The packaging of the 39.937-kbp DNA genome of the short-tail Escherichia coli bacteriophage, T7, is a model for understanding basic principles common to dsDNA tailed phages and herpes viruses. The T7 system is also of interest because it has been used for popular biotechnologies, such as recombinant protein expression (10) and protein display on the capsid surface (11). The T7 capsid contains 415 copies of the major shell protein gp10 (12) that form a T = 7L icosahedral lattice. From low-resolution cryo-EM 3D reconstructions the tertiary topology of gp10 can be divided into four regions: N-arm, E-loop, A-domain, and P-domain, which together place the gp10 protein in the HK97 fold category (2, 13, 14). The T7 procapsid, capsid I, contains 110–140 molecules of scaffolding protein, gp9 (4, 15, 16). After scaffolding protein expulsion the spherical T7 capsid I expands to more angular intermediates, which are collectively called capsid II (2, 4, 14, 16–18).Two DNA-free capsid IIs are purified in quantity sufficient for structural studies by cryo-EM (16). Both are produced during the normal process of wild-type T7 DNA packaging in vivo. One has an unusually low density during buoyant density centrifugation in a metrizamide density gradient (1.086 g/mL; metrizamide low density, or MLD, capsid II) and the other has a density as expected for hydrated proteins (1.28 g/mL; metrizamide high density, or MHD, capsid II) (16). The low density of MLD capsid II is caused by impermeability to metrizamide (789 Da) (16). The MLD capsid II particles are produced before MHD capsid II particles based on kinetic studies (16).The DNA packaging of T7 phage starts at capsid I state where the DNA is packaged by the ATPases (gp18 and gp19) to pass through the portal (gp8) apparatus (19). By analyzing kinetics of in vivo-produced capsids, MLD capsid II was found to be the first postcapsid I capsid. MLD capsid II appears with the kinetics of an intermediate (16) but is obviously no longer in the DNA packaging pathway because it has detached from the DNA molecule that it was packaging. MLD capsid II is not produced when a nonpermissive host is infected with a T7 amber mutant defective in DNA packaging (summarized in ref. 16). Thus, MLD capsid II is an intermediate that has been altered during either cellular lysis or subsequent purification. MHD capsid II also has the appearance kinetics of an intermediate of packaging, but one that occurs later (16). Whereas MLD capsid II has the internal core stack including proteins gp8, gp14, gp15, and gp16 (16), MHD capsid II does not have the internal core stack proteins, which were presumably lost when packaged DNA exited the capsid (16).The existence of these various capsids provides an opportunity to obtain a high-resolution (3–4 Å) analysis of structural dynamics that occur in vivo. Here we report cryo-EM structures of the shells of the following bacteriophage T7 capsids: capsid I (4.6 Å), MLD capsid II (3.5 Å), MHD capsid II (6.6 Å), and phage (3.6 Å). The two capsid II shells are the first postprocapsid, in vivo-generated shells (for any packaging system) to be subjected to high-resolution structural analysis, to our knowledge. The results reveal (i) an HK97-fold shell protein with an intracapsomere, noncovalent topological linking and another intercapsomere, joint interaction, neither interaction having been found for other dsDNA tailed phages; (ii) details of the interaction of gp9 scaffolding protein with the inner surface of the capsid I shell; (iii) a novel refolding and externalization of the N terminus of major capsid protein, gp10; and (iv) a subtle, surprising contraction of the gp10 shell in transit from MLD capsid II to phage. Based on these observations, we propose a general procapsid assembly and maturation pathway for dsDNA viruses.