Pub Date : 1975-01-01DOI: 10.1007/978-1-4684-7668-2_6
E. Neumann, D. Nachmansohn
{"title":"Nerve excitability--toward an integrating concept.","authors":"E. Neumann, D. Nachmansohn","doi":"10.1007/978-1-4684-7668-2_6","DOIUrl":"https://doi.org/10.1007/978-1-4684-7668-2_6","url":null,"abstract":"","PeriodicalId":75600,"journal":{"name":"Biomembranes","volume":"99 1","pages":"99-166"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51022164","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1975-01-01DOI: 10.1007/978-1-4684-7668-2_5
I Goldberg, I Friedberg, I Ohad
The light-induced formation of the photosynthetic membranes (greening) in y-1 mutant of Chlamydomonas reinhardi requires synthesis of new proteins which become incorporated into the growing membranes. It has been shown previously (Eytan and Ohad, 1970) that proteins synthesized by both chloroplast and cytoplasmic ribosomes concur in the formation of functional photosynthetic membranes, indicating the presence of a mechanism permitting the specific transfer of membrane proteins synthesized in the cytoplasm into the chloroplast. Transfer of such proteins cannot yet be identified by the usual biochemical techniques unless they become part of the growing photosynthetic membranes. However, it is possible to follow their synthesis and translocation between the different cellular compartments by use of quantitative electron microscopic radioautography. In the present work, the radioautographic grain distribution among chloroplast, chloroplast membrane, nucleus, mitochondria, and the remainder of the cytoplasm (cytosol) was carried out following short radioactive pulse-labeling and chase during greening of dark-grown mutants in the presence or absence of protein synthesis inhibitors. The results indicate that transport of some of the proteins of cytoplasmic origin to their final location within the chloroplast is at least partially controlled by concomitant synthesis of proteins by the chloroplast ribosomes.
{"title":"Biogenesis of chloroplast membranes in Chlamydomonas reinhardi: Chloroplast-controlled transfer of cytoplasmic proteins to the developing chloroplast membranes as visualized by quantitative radioautography.","authors":"I Goldberg, I Friedberg, I Ohad","doi":"10.1007/978-1-4684-7668-2_5","DOIUrl":"https://doi.org/10.1007/978-1-4684-7668-2_5","url":null,"abstract":"<p><p>The light-induced formation of the photosynthetic membranes (greening) in y-1 mutant of Chlamydomonas reinhardi requires synthesis of new proteins which become incorporated into the growing membranes. It has been shown previously (Eytan and Ohad, 1970) that proteins synthesized by both chloroplast and cytoplasmic ribosomes concur in the formation of functional photosynthetic membranes, indicating the presence of a mechanism permitting the specific transfer of membrane proteins synthesized in the cytoplasm into the chloroplast. Transfer of such proteins cannot yet be identified by the usual biochemical techniques unless they become part of the growing photosynthetic membranes. However, it is possible to follow their synthesis and translocation between the different cellular compartments by use of quantitative electron microscopic radioautography. In the present work, the radioautographic grain distribution among chloroplast, chloroplast membrane, nucleus, mitochondria, and the remainder of the cytoplasm (cytosol) was carried out following short radioactive pulse-labeling and chase during greening of dark-grown mutants in the presence or absence of protein synthesis inhibitors. The results indicate that transport of some of the proteins of cytoplasmic origin to their final location within the chloroplast is at least partially controlled by concomitant synthesis of proteins by the chloroplast ribosomes.</p>","PeriodicalId":75600,"journal":{"name":"Biomembranes","volume":"7 ","pages":"81-98"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12304001","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Electrochromic properties of membrane probes.","authors":"W K Cheng","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":75600,"journal":{"name":"Biomembranes","volume":"7 ","pages":"56-60"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12304000","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1975-01-01DOI: 10.1007/978-1-4684-7668-2_4
A Frenkel, E B Ekblad, I S Edelman
The role of reactive SH groups (presumably in proteins) of the apical plasma membrane in transepithelial Na+ transport was studied in the isolated urinary bladder of the toad. On the basis of assays for TCA-soluble SH compounds (e.g., glutathione, methionine), PCMB, PCMPS, NTCB, and DTNB did not penetrate the intracellular compartment from the luminal media either in control or vasopressin-treated bladders. In contrast, PCMB from the serosal side and NEM from the luminal side titrated significant fractions of the TCA-soluble SH compounds. We conclude, therefore, the PCMB, PCMPS, NTCB, and DTNB are suitable reagents for studies on the physiological properties of apical plasma membrane SH groups. Titration of apical membrane SH groups with PCMPS, NTCB, and DTNB revealed heterogeneity in functional responses: PCMPS and NTCB elicited transient, 25-60% increases in SCC. In substrate-free media, pretreatment with these reagents inhibited the increase in SCC produced by vasopressin or cyclic AMP (+ theophylline). In glucose-enriched media, the responses to combinations of vasopressin and PCMPS or NTCB were additive, implying activation via parallel pathways. Simultaneous addition of vasopressin or cyclic AMP (+ theophylline) and NTCB resulted in marked synergism, presumably as a result of unmasking of SH groups by the the hormone (or the intermediate). These results suggest that basal Na+ transport is regulated in part by SH compounds in the apical membrane that are distinct, although not necessarily different in kind, from those involved in the response to vasopressin.
{"title":"Effects of sulfhydryl reagents on basal and vasopressin-stimulated Na+ transport in the toad bladder.","authors":"A Frenkel, E B Ekblad, I S Edelman","doi":"10.1007/978-1-4684-7668-2_4","DOIUrl":"https://doi.org/10.1007/978-1-4684-7668-2_4","url":null,"abstract":"<p><p>The role of reactive SH groups (presumably in proteins) of the apical plasma membrane in transepithelial Na+ transport was studied in the isolated urinary bladder of the toad. On the basis of assays for TCA-soluble SH compounds (e.g., glutathione, methionine), PCMB, PCMPS, NTCB, and DTNB did not penetrate the intracellular compartment from the luminal media either in control or vasopressin-treated bladders. In contrast, PCMB from the serosal side and NEM from the luminal side titrated significant fractions of the TCA-soluble SH compounds. We conclude, therefore, the PCMB, PCMPS, NTCB, and DTNB are suitable reagents for studies on the physiological properties of apical plasma membrane SH groups. Titration of apical membrane SH groups with PCMPS, NTCB, and DTNB revealed heterogeneity in functional responses: PCMPS and NTCB elicited transient, 25-60% increases in SCC. In substrate-free media, pretreatment with these reagents inhibited the increase in SCC produced by vasopressin or cyclic AMP (+ theophylline). In glucose-enriched media, the responses to combinations of vasopressin and PCMPS or NTCB were additive, implying activation via parallel pathways. Simultaneous addition of vasopressin or cyclic AMP (+ theophylline) and NTCB resulted in marked synergism, presumably as a result of unmasking of SH groups by the the hormone (or the intermediate). These results suggest that basal Na+ transport is regulated in part by SH compounds in the apical membrane that are distinct, although not necessarily different in kind, from those involved in the response to vasopressin.</p>","PeriodicalId":75600,"journal":{"name":"Biomembranes","volume":"7 ","pages":"61-80"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11383511","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Bacterial membranes and the respiratory chain.","authors":"N S Gel'man, M A Lukoyanova, D N Ostrovskii","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":75600,"journal":{"name":"Biomembranes","volume":"6 ","pages":"1-261"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12369176","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1975-01-01DOI: 10.1007/978-1-4684-7668-2_1
D Chapman
{"title":"Fluidity and phase transitions of cell membranes.","authors":"D Chapman","doi":"10.1007/978-1-4684-7668-2_1","DOIUrl":"https://doi.org/10.1007/978-1-4684-7668-2_1","url":null,"abstract":"","PeriodicalId":75600,"journal":{"name":"Biomembranes","volume":"7 ","pages":"1-9"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-1-4684-7668-2_1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12271737","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Although numerous experimental data have been accumulated in the various fields of research on bioelectricity, the mechanism of nerve excitability is still an unsolved problem. Many mechanistic interpretations of nerve behavior cover only a part of the facts, are thus selective and unsatisfactory. An attempt at an integral interpretation of basic data well-established by electrophysiological, biochemical, and biophysical investigations was inspired by the late Aharon Katchalsky and a first attempt had been made previously (Neumann et al., 1973). The present account is a further step toward a quantitative physiochemical theory of bioelectricity. We have further explored the previously introduced notion of a basic excitation unit in excitable membranes. This notion is of fundamental importance for modeling details of sub- and suprathreshold responses, such as threshold behavior and strength-duration curves, in terms of kinetic parameters for specific membrane processes. Our integral model of excitability is based on the original chemical hypothesis for the control of bioelectricity (Nachmansohn, 1959, 1971b). This specific approach includes some frequently ignored experimental facts on acetylcholine-processing proteins in excitable membranes. According to the integral model, acetylcholine ions are continuously processed through the basic excitation units within excitable membranes: axonal, presynaptic, and postsynaptic parts. Excitability, i.e., the generation and propagation of nerve impulses, is due to a cooperative increase in the rate of AcCh translocation through the cholinergic control system.
虽然在生物电的各个研究领域已经积累了大量的实验数据,但神经兴奋性的机制仍然是一个未解决的问题。许多对神经行为的机械性解释只涵盖了部分事实,因此是选择性的和不令人满意的。对电生理学、生物化学和生物物理学研究中建立的基本数据进行整体解释的尝试是受到已故的Aharon Katchalsky的启发,并且之前已经进行了第一次尝试(Neumann et al., 1973)。本报告是向定量的生物电物理化学理论又迈进了一步。我们进一步探讨了先前介绍的可兴奋膜中基本激发单元的概念。这一概念对于模拟亚阈值和超阈值响应的细节至关重要,例如阈值行为和强度-持续时间曲线,以及特定膜过程的动力学参数。我们的兴奋性积分模型是基于控制生物电的原始化学假设(Nachmansohn, 1959, 1971b)。这种特殊的方法包括一些经常被忽视的关于可兴奋膜中乙酰胆碱加工蛋白的实验事实。根据积分模型,乙酰胆碱离子通过可兴奋膜内的基本兴奋单元(轴突、突触前和突触后部分)连续加工。兴奋性,即神经冲动的产生和传播,是由于乙酰胆碱能控制系统协同增加乙酰胆碱转运的速率。
{"title":"Nerve excitability--toward an integrating concept.","authors":"E Neumann, D Nachmansohn","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Although numerous experimental data have been accumulated in the various fields of research on bioelectricity, the mechanism of nerve excitability is still an unsolved problem. Many mechanistic interpretations of nerve behavior cover only a part of the facts, are thus selective and unsatisfactory. An attempt at an integral interpretation of basic data well-established by electrophysiological, biochemical, and biophysical investigations was inspired by the late Aharon Katchalsky and a first attempt had been made previously (Neumann et al., 1973). The present account is a further step toward a quantitative physiochemical theory of bioelectricity. We have further explored the previously introduced notion of a basic excitation unit in excitable membranes. This notion is of fundamental importance for modeling details of sub- and suprathreshold responses, such as threshold behavior and strength-duration curves, in terms of kinetic parameters for specific membrane processes. Our integral model of excitability is based on the original chemical hypothesis for the control of bioelectricity (Nachmansohn, 1959, 1971b). This specific approach includes some frequently ignored experimental facts on acetylcholine-processing proteins in excitable membranes. According to the integral model, acetylcholine ions are continuously processed through the basic excitation units within excitable membranes: axonal, presynaptic, and postsynaptic parts. Excitability, i.e., the generation and propagation of nerve impulses, is due to a cooperative increase in the rate of AcCh translocation through the cholinergic control system.</p>","PeriodicalId":75600,"journal":{"name":"Biomembranes","volume":"7 ","pages":"99-166"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12273317","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1975-01-01DOI: 10.1007/978-1-4684-7668-2_3
B Chance
{"title":"Carotenoid and merocyanine probes in chromatophore membranes.","authors":"B Chance","doi":"10.1007/978-1-4684-7668-2_3","DOIUrl":"https://doi.org/10.1007/978-1-4684-7668-2_3","url":null,"abstract":"","PeriodicalId":75600,"journal":{"name":"Biomembranes","volume":"7 ","pages":"33-55"},"PeriodicalIF":0.0,"publicationDate":"1975-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11993045","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}