不同ATP浓度对牛蛙离体腓肠肌收缩性的影响

通过对牛蛙腓肠肌收缩性的研究,将接受连续刺激产生疲劳后的腓肠肌浸泡在不同浓度的ATP中,利用LMS-2B型二道生理纪录仪记录腓肠肌在不同ATP浓度中消除疲劳后的收缩强度和疲劳时间,观察不同浓度的ATP(2%、3%、4%)对接受连续刺激产生疲劳后的腓肠肌收缩能力的影响.实验结果显示:使牛蛙腓肠肌收缩能力最佳的ATP浓度为3%.     

ATP与生命活动中能量的供应

在ATP中,活跃的化学能以高能磷酸键的形式储存,在生物有机体中,肌肉的收缩,主动运输,生物发光都需要ATP,ATP与物质代谢关系密切.     

Q：为什么剧烈运动后，第二天起床会感到浑身酸痛？

A：这种症状一般出现在久未运动的人身上,医学上称之为延迟性肌肉酸痛。众所周知,运动的力量来自于肌肉的收缩,而肌肉的收缩涉及到非常复杂的化学变化,其中所需能量来自体内三磷酸腺苷（ATP）的分解。再向上追溯,ATP又来自机体对糖类的分解。糖类分解分为有氧和无氧两种情况。糖类首先被分解为丙酮酸,在有氧过程中,丙酮酸被分解为二氧化碳和水,并释放大量ATP,但在剧烈运动时,肌肉需要大量的能量供应,因此需氧量也急剧增加。     

肌肉自发振动过程中结合几率与化学反应速率的变化

定量分析肌球蛋白与肌动蛋白丝的结合几率及相关化学反应的速率常数,对于准确掌握肌肉收缩的内在机制具有非常重要的意义.以肌肉自发振动的实验结果为依据,从振动过程所满足的动力学方程出发,推导出结合几率与肌丝滑行速度及肌节长度之间的定量关系,并求得化学反应速率随肌肉收缩的速度变化而改变的数学规律.结果显示,结合几率的基准值由溶液中主要化学成分的浓度决定;结合几率的变化值与肌肉收缩的速度成正比,与肌节长度成反比;而化学反应速率随收缩速度按指数规律变化.上述结果与实验值基本一致.     

过度代谢与运动能力的关系

采用文献综述研究方法,论述了糖、氨和ATP过度代谢对机体正常功能的影响,探讨了其对运动能力的作用机制.资料表明,糖的过度代谢致使机体pH值下降,导致糖代谢关键酶的活性下降,肌肉收缩能力降低,ATP合成及水解释放自由能减少;氨的过度产生可造成中枢神经疲劳,对某些生化反应具有不良影响;ATP的过度利用会引起机体正常生物学功能受损.上述生物化学变化会使人体运动能力显著下降.     

苯乙烯-甲基丙烯酸甲酯-丙烯醛三元无皂乳液共聚合动力学研究

以苯乙烯 (St)、甲基丙烯酸甲酯 (MMA)为主单体 ,丙烯醛 (AL)为功能单体进行了无皂乳液批量共聚合 .考察了功能单体浓度、引发剂过硫酸铵ATP浓度及聚合温度对其动力学行为的影响 ,用Gamma积分函数拟合了转化率 -时间关系曲线 ,获得了聚合过程的重要特征参数如 :平均成核速率 (Nv) ,聚合最大速率(Mv)和平稳期平均聚合速率 (Av)及成核结束和聚合进入完成期对应的转化率 .同时对聚合速率与以上各聚合参数的关系数据进行了非线性拟合 ,得到了聚合速率与以上各单个聚合参数的关系式及综合关系式 .结果表明 :聚合速率随功能单体浓度、ATP浓度及聚合温度增大而增大 ,但增大幅度逐渐减小 ;聚合过程中ATP起决定作用 .     

肌肉训练的生理学分析

本文从生理学的角度,对肌肉的收缩过程,肌肉训练三要素及不同肌肉训练方法进行分析,为肌肉力量训练提供了生理依据。     

肌酸激酶的生理功能与运动

肌酸激酶(creatine kinase,CK)是催化磷酸肌酸和ATP间高能磷酸基团转移的关键酶,它保持ATP/ADP比例平衡和ATP的供给。肌酸激酶家族共有5种同工酶,分布于全身各种组织的需能部位。研究发现,CK酶在能量代谢中有重要作用,与肌肉收缩、神经功能、细胞膜的稳定性、细胞的能量反馈调节、有氧耐力有关。一些研究认为,CKM(肌型肌酸激酶,creatine kinase,muscle)基因多态性影响个体有氧运动能力和个体对耐力训练的敏感性。本文对这些成果作一综述,并对未来研究进行展望,以期为进一步的研究提供参考。     

SIOC-AA-005的抗肿瘤作用机制研究

探讨SIOC-AA-005抗肿瘤的作用机制.采用测定HT-29 细胞线粒体膜流动性、线粒体ATP含量、线粒体ATP酶活性及NADH-CoQ氧化还原酶活性、细胞质膜NADH氧化酶活性的方法,对其作用机制进行了深入探讨;SIOC-AA-005在10 nmol/L剂量下可明显降低线粒体膜的流动性,并使线粒体膜电位显著升高;在此浓度下,SIOC-AA-005还可使HT-29细胞内的ATP耗竭,ATP酶活性受到抑制,线粒体中能量产生过程受阻.在胞外反应体系中,SIOC-AA-005对NADH-CoQ氧化还原酶有强烈的抑制作用,对细胞质膜NADH氧化酶也具有较强的抑制作用.SIOC-AA-005可能是通过抑制线粒体NADH-CoQ氧化还原酶、抑制细胞质膜NADH氧化酶以及线粒体ATP酶活性,从而使线粒体膜流动性下降,膜电位升高,细胞内ATP耗竭,最终使肿瘤细胞死亡。     

短跑放松技术训练方法探讨

当今短跑比赛竞争越来越激烈，胜负的差距往往在1／100秒甚至1／1000秒。运动生理学指出：支持肌肉快速收缩的能量要靠ATP-CP系统的分解合成来供给，而CP促使ADP再次合成ATP往往是在肌肉的放松状态下。由此可见，短跑的放松技术是维持高速跑进和提高成绩的重要条件。本文将对放松技术及其训练方法进行探讨。     

Effects of ATP and vanadate on calcium efflux from barnacle muscle fibres

Calcium ions carry the inward current during depolarization of barnacle muscle fibres and are involved in the contraction process. Intracellular ionized calcium ([Ca2+]i) in barnacle muscle, as in other cells, is kept at a very low concentration, against a large electrochemical gradient. This large gradient is maintained by Ca2+ extrusion mechanisms. When [Ca2+]i is below the contraction threshold, Ca2+ efflux from giant barnacle muscle fibres is, largely, both ATP dependent and external Na+ (Na+0) dependent (see also refs 5,6). When [Ca2+]i is raised to the level expected during muscle contraction (2-5 muM), most of the Ca2+ efflux from perfused fibres is Na0 dependent; as in squid axons, this Na+0-dependent Ca2+ efflux is ATP independent. Orthovanadate is an inhibitor of (Na+ + K+) ATPase and the red cell Ca2+-ATpase. We report here that vanadate inhibits ATP-promoted, Na+0-dependent Ca2+ efflux from barnacle muscle fibres perfused with low [Ca2+]i (0.2-0.5 microM), but has little effect on the Na+0-dependent, ATP-independent Ca2+ efflux from fibres with a high [Ca]i (2-5 microM). Nevertheless, ATP depletion or vanadate treatment of high [Ca2+]i fibres causes an approximately 50-fold increase of Ca2+ efflux into Ca2+-containing lithium seawater. These results demonstrate that both vanadate and ATP affect Ca2+ extrusion, including the Na+0-dependent Ca2+ efflux (Na-Ca exchange), in barnacle muscle.     

Rapid regeneration of the actin-myosin power stroke in contracting muscle.

At the molecular level, muscle contraction is the result of cyclic interaction between myosin crossbridges, which extend from the thick filament, and the thin filament, which consists mainly of actin. The energy for work done by a single crossbridge during a cycle of attachment, generation of force, shortening and detachment is believed to be coupled to the hydrolysis of one molecule of ATP. The distance the actin filament slides relative to the myosin filament in one crossbridge cycle has been estimated as 12 nm by step-length perturbation studies on single fibres from frog muscle. The 'mechanical' power stroke of the attached crossbridge can therefore be defined as 12-nm shortening with a force profile like that shown by the quick recovery of force following a length perturbation. According to this definition, power strokes cannot be repeated faster than the overall ATPase rate. Here, however, we show that the power stroke can be regenerated much faster than expected from the ATPase rate. This contradiction can be resolved if, in the shortening muscle, the free energy of ATP hydrolysis is used in several actin-myosin interactions consisting of elementary power strokes each of 5-10 nm.     

Modulation of ATP-sensitive K+ channels in skeletal muscle by intracellular protons

Since their discovery in cardiac muscle, ATP-sensitive K+(KATP) channels have been identified in pancreatic beta-cells, skeletal muscle, smooth muscle and central neurons. The activity of KATP channels is inhibited by the presence of cytosolic ATP. Their wide distribution indicates that they could have important physiological roles that may vary between tissues. In muscle cells the role of K+ channels is to control membrane excitability and the duration of the action potential. In anoxic cardiac ventricular muscle KATP channels are believed to be responsible for shortening the action potential, and it has been proposed that a fall in ATP concentration during metabolic exhaustion increases the activity of KATP channels in skeletal muscle, which may reduce excitability. But the intracellular concentration of ATP in muscle is buffered by creatine phosphate to 5-10 mM, and changes little, even during sustained activity. This concentration is much higher than the intracellular ATP concentration required to half block the KATP-channel current in either cardiac muscle (0.1 mM) or skeletal muscle (0.14 mM), indicating that the open-state probability of KATP channels is normally very low in intact muscle. So it is likely that some additional means of regulating the activity of KATP channels exists, such as the binding of nucleotides other than ATP. Here I present evidence that a decrease in intracellular pH (pHi) markedly reduces the inhibitory effect of ATP on these channels in excised patches from frog skeletal muscle. Because sustained muscular activity can decrease pHi by almost 1 unit in the range at which KATP channels are most sensitive to pHi, it is likely that the activity of these channels in skeletal muscle is regulated by intracellular protons under physiological conditions.     

Sliding distance of actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle

Muscle contraction results from a sliding movement of actin filaments induced by myosin crossbridges on hydrolysis of ATP, and many non-muscle cells are thought to move using a similar mechanism. The molecular mechanism of muscle contraction, however, is not completely understood. One of the major problems is the mechanochemical coupling at high velocity under near-zero load. Here, we report measurements of the sliding distance of an actin filament induced by a myosin crossbridge during one ATP hydrolysis cycle in an unloaded condition. We used single sarcomeres from which the Z-lines, structures which anchor the thin filaments in the sarcomere, had been completely removed by calcium-activated neutral protease (CANP) and trypsin, and measured both the sliding velocity of single actin filaments along myosin filaments and the ATPase activity during sliding. Our results show that the average sliding distance of the actin filament is less than or equal to 600 A during one ATP cycle, much longer than the length of power stroke of myosin crossbridges deduced from mechanical studies of muscle, which is of the order of 80 A (for example, ref. 15).     

Effects of modulators of myosin light-chain kinase activity in single smooth muscle cells

Phosphorylation of myosin light chains by a calmodulin-myosin light-chain kinase (MLCK) pathway is considered to be responsible for coupling increased calcium concentration with contraction in smooth muscle. This simple view has, however, recently been questioned. To test this hypothesis directly, we microinjected individual smooth muscle cells with modulators of the MLCK pathway while measuring contraction and calcium-ion concentration. Injection of a constitutively active proteolyzed form of MLCK causes contraction but no change in calcium concentration. By contrast, injection of peptide inhibitors of MLCK blocks contraction in response to K+ depolarization, despite the fact that the change in calcium concentration in response to stimulation was enhanced over controls. These results provide a direct demonstration at the level of a single cell that activation of the calmodulin-MLCK pathway is both necessary and sufficient to trigger contraction of smooth muscle.     

核能补剂对大鼠骨骼肌高能磷酸化合物变化的影响

通过实验观察了核能补剂对大鼠骨骼肌高能磷酸化合物变化的影响。大鼠反复进行3次2min的高速跑台运动,其运动后第24h腓肠肌中高能磷酸化合物的变化提示:核能补剂组骨骼肌中ATP的含量明显比复合肌酸组和空白对照组高(p<0.01);核能补剂组骨骼肌中PCr的含量明显比空白对照组高(p<0.01)。本实验证实了核能补剂能加快骨骼肌ATP的生成速度,并提高骨骼肌中磷酸肌酸的储量。     

Myosin phosphorylation, agonist concentration and contraction of tracheal smooth muscle

Myosin phosphorylation plays an important part in excitation--contraction coupling in smooth muscle. Phosphorylation by a Ca2+, calmodulin-dependent kinase stimulates the actin-activated Mg2+-ATPase activity of smooth muscle myosin, suggesting that myosin phosphorylation regulates smooth muscle contraction. This hypothesis is supported by evidence that myosin is phosphorylated during contraction and dephosphorylated during relaxation of intact smooth muscles stimulated with a single agonist concentration. However, there is little information regarding the response to stimulation with various agonist concentrations. As the dose-response relationships for phosphorylation and tension should be similar if myosin phosphorylation does, in fact, regulate smooth muscle contraction, we studied myosin phosphorylation in tracheal smooth muscle stimulated with a broad range of concentrations of the cholinergic agonist, methacholine. The results of these experiments are consistent with the hypothesis that myosin phosphorylation regulates smooth muscle contraction but they indicate a relatively complex relationship between myosin phosphorylation and the generation of isometric tension.     

The motor protein myosin-I produces its working stroke in two steps

Many types of cellular motility, including muscle contraction, are driven by the cyclical interaction of the motor protein myosin with actin filaments, coupled to the breakdown of ATP. It is thought that myosin binds to actin and then produces force and movement as it 'tilts' or 'rocks' into one or more subsequent, stable conformations. Here we use an optical-tweezers transducer to measure the mechanical transitions made by a single myosin head while it is attached to actin. We find that two members of the myosin-I family, rat liver myosin-I of relative molecular mass 130,000 (M(r) 130K) and chick intestinal brush-border myosin-I, produce movement in two distinct steps. The initial movement (of roughly 6 nanometres) is produced within 10 milliseconds of actomyosin binding, and the second step (of roughly 5.5 nanometres) occurs after a variable time delay. The duration of the period following the second step is also variable and depends on the concentration of ATP. At the highest time resolution possible (about 1 millisecond), we cannot detect this second step when studying the single-headed subfragment-1 of fast skeletal muscle myosin II. The slower kinetics of myosin-I have allowed us to observe the separate mechanical states that contribute to its working stroke.     

分子筛在苏云金芽孢杆菌发酵液浓缩中的应用研究

本文观察了不同孔径分子筛对 B.t.发酵液的浓缩效果 ,结果表明 6 0 0 - 5 0万 Da这 9种规格孔径的分子筛膜的滤出液都检测不到晶体和细胞的存在 ,晶体和芽胞的回收率为 10 0 %。但超滤液通量随着膜孔径增大而增大。发酵液固形物含量越低 ,分离时间越短 ,浓缩比越高 ,当固形物含量在 1.5 %时 ,分离时间为2 0 min,浓缩比为 8.6 6 7;而固形物含量为 15 %时 ,分离时间延长到 6 9min,浓缩比降为 1.348。浓缩效果还受待浓缩液通过分子筛速度的影响。     

基于互Wigner-Ville分布的表面肌电信号瞬时频率估计

当一块肌肉完成持续的收缩时,所记录的表面肌电信号的分析是一个用于评价局部疲劳进行性的有用的工具.在肌肉静态收缩期间,表面肌电信号功率谱的平均频率和中值频率常被用作肌肉疲劳的指示器.为了评价周期性动态收缩期间的局部肌肉疲劳,针对肌肉动态收缩时表面肌电信号的特点,提出了基于互Wigner-Ville分布的瞬时频率检测方法.通过一个类似于表面肌电信号统计性质的模拟的随机过程,评价了这一算法的估计误差.理论和实验证明,瞬时频率可以在较低的信噪比下很好地适合跟踪由于肌肉疲劳引起的频谱变化.