The channel-forming antibiotic gramicidin A increases the K+ conductance of frog skeletal muscle fibres in isotonic K2SO4 solution. The conductance of the gramicidin channel is not affected by Rb+ or Cs+, but is reduced by T1+. In contrast, the conductance of the normal K+ channel is decreased by Rb+ and Cs+ but is nearly unaffected by 5 and 10 mM T1+. The results suggest differences in the cation permeation through the gramicidin and the K+ channel of the muscle cell membrane.
在等渗K2SO4溶液中,形成通道的抗生素革兰霉素A增加了青蛙骨骼肌纤维的K+电导。gramicidin通道的电导不受Rb+或Cs+的影响,但受T1+的影响而降低。相比之下,正常K+通道的电导被Rb+和Cs+降低,但几乎不受5和10 mM T1+的影响。结果表明,通过革兰霉素通道和肌细胞膜的K+通道的阳离子渗透存在差异。
{"title":"The effect of Rb+, Cs+, and T1+ on the gramicidin A-induced conductance changes of the skeletal muscle cell membrane.","authors":"G Caffier, N E Shvinka","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The channel-forming antibiotic gramicidin A increases the K+ conductance of frog skeletal muscle fibres in isotonic K2SO4 solution. The conductance of the gramicidin channel is not affected by Rb+ or Cs+, but is reduced by T1+. In contrast, the conductance of the normal K+ channel is decreased by Rb+ and Cs+ but is nearly unaffected by 5 and 10 mM T1+. The results suggest differences in the cation permeation through the gramicidin and the K+ channel of the muscle cell membrane.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 11","pages":"1087-90"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17254142","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}
An ouabain-insensitive, Mg++-dependent, Na+-stimulated ATPase activity which is inhibited by furosemide was found in mucosal homogenate of rat small intestine. The subcellular localization of this ATPase activity was studied by means of isolated purified brush borders and basolateral plasma membranes. The results suggest a nearly identical distribution of Na+-activated and (Na+K+)-activated ATPase within the epithelial cells. Under conditions of alloxan and streptozotocin diabetes an increase of both ATPase activities can be found only in the basolateral plasma membranes. These observations agree well with the convective model of intestinal absorption.
{"title":"[Detection of a Na+-activated, furosemide-inhibited ATPase activity in rat intestinal mucosa].","authors":"D Luppa, F Müller","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>An ouabain-insensitive, Mg++-dependent, Na+-stimulated ATPase activity which is inhibited by furosemide was found in mucosal homogenate of rat small intestine. The subcellular localization of this ATPase activity was studied by means of isolated purified brush borders and basolateral plasma membranes. The results suggest a nearly identical distribution of Na+-activated and (Na+K+)-activated ATPase within the epithelial cells. Under conditions of alloxan and streptozotocin diabetes an increase of both ATPase activities can be found only in the basolateral plasma membranes. These observations agree well with the convective model of intestinal absorption.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 11","pages":"1037-43"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17285579","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}
K Hecht, H Hilse, A M Aquino, P Oehme, L Piesche, M Poppei
The norepinephrine content of neocortex, hippocampus, and adrenals of adult male Wistar rats was estimated. In normal rats an asymmetrical right-left-distribution of the norepinephrine content was found. Neocortex and hippocampus showed a contralateral, neocortex and adrenals an ipsilateral ratio. Chronic stress cancelled this right-left asymmetry of norepinephrine distribution. In brain the levelling appeared earlier than in adrenals.
{"title":"[Asymmetrical distribution of noradrenaline in the neocortex, hippocampus and adrenal glands of rats and changes with chronic activity restriction].","authors":"K Hecht, H Hilse, A M Aquino, P Oehme, L Piesche, M Poppei","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The norepinephrine content of neocortex, hippocampus, and adrenals of adult male Wistar rats was estimated. In normal rats an asymmetrical right-left-distribution of the norepinephrine content was found. Neocortex and hippocampus showed a contralateral, neocortex and adrenals an ipsilateral ratio. Chronic stress cancelled this right-left asymmetry of norepinephrine distribution. In brain the levelling appeared earlier than in adrenals.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 7-8","pages":"641-5"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18163792","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}
Using a microelectrode technique the influence of experimental conditions which are known to alter the intracellular free Ca concentration upon the repolarization phase in the rabbit atrial myocardium was studied. Under all the tested conditions (increased external Ca concentration, application of ouabain, decreased external K concentration) a positive inotropic effect was observed. The action potentials showed a rapid initial repolarization. The positive inotropic effect was found to be well correlated with the effect of the action potential's shortening at 25% repolarization. After pacing pauses a positive correlation between the velocity of the initial rapid repolarization and the potentiation of the atrial contraction was established. It is discussed that all the conditions were able to increase the internal Ca concentration and that in consequence of it a CA-sensitive outward current at potentials about 40 mV more positive than the resting potential is activated.
{"title":"Does a calcium-mediated outward current exist in the atrial myocardium?","authors":"B Nilius, K Schüttler, W Boldt","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Using a microelectrode technique the influence of experimental conditions which are known to alter the intracellular free Ca concentration upon the repolarization phase in the rabbit atrial myocardium was studied. Under all the tested conditions (increased external Ca concentration, application of ouabain, decreased external K concentration) a positive inotropic effect was observed. The action potentials showed a rapid initial repolarization. The positive inotropic effect was found to be well correlated with the effect of the action potential's shortening at 25% repolarization. After pacing pauses a positive correlation between the velocity of the initial rapid repolarization and the potentiation of the atrial contraction was established. It is discussed that all the conditions were able to increase the internal Ca concentration and that in consequence of it a CA-sensitive outward current at potentials about 40 mV more positive than the resting potential is activated.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 6","pages":"553-63"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18163908","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}
Rye germ lectin was isolated by extraction of defatted rye germ, fractionation of the extract by ammonium sulfate precipitation, affinity chromatography of the active substances on chitin-beta-glucan and gel filtration on Sephadex G-50. The lectin shows erythroagglutinating activity at a minimum concentration of 2.5 micrograms/ml. The erythroagglutinating activity is the same against human red blood cells of all types of the ABO system and is inhibited by N-acetyl-D-glucosamine. The lectin has no mitogenic activity against mouse splenic lymphocytes. According to the results of polyacrylamide gel electrophoresis the lectin obtained is a mixture of three very similar isolectins of equal erythroagglutinating activity. Sedimentation analysis indicates homogeneity of the lectin preparation; the molecular weight was 56000 as estimated by sedimentation equilibrium. In the presence of urea and sodium dodecyl sulfate the lectin dissociates into 2 types of subunits with molecular weights of 35000 and 19000. The rye germ lectin contains about 2% of neutral sugar and 1% of D-glucosamine. The amino acid composition of the lectin is characterized by a very high content of glycine and half cystine and a low content of apolar amino acids. N-terminal amino acids of the lectin are apparently blocked.
采用脱脂黑麦胚芽提取、硫酸铵沉淀法分离、甲壳素-葡聚糖亲和层析、Sephadex G-50凝胶过滤等方法分离黑麦胚芽凝集素。凝集素在最低浓度为2.5微克/毫升时显示出红细胞凝集活性。红细胞凝集活性对所有ABO系统类型的人红细胞是相同的,并被n -乙酰- d -氨基葡萄糖抑制。凝集素对小鼠脾淋巴细胞无促有丝分裂活性。根据聚丙烯酰胺凝胶电泳的结果,所得的凝集素是三种非常相似的、具有相同红细胞凝集活性的分离素的混合物。沉淀分析表明凝集素制备的均匀性;经沉淀平衡计算,分子量为56000。在尿素和十二烷基硫酸钠存在下,凝集素解离成两种分子量分别为35000和19000的亚基。黑麦胚芽凝集素含有约2%的中性糖和1%的d -氨基葡萄糖。凝集素的氨基酸组成特点是甘氨酸和半胱氨酸含量很高,极性氨基酸含量很低。凝集素的n端氨基酸明显受阻。
{"title":"Studies on lectins. LII. Isolation and characterization of the lectin from rye germ (Secale cereale L.).","authors":"J Kubánek, G Entlicher, J Kocourek","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Rye germ lectin was isolated by extraction of defatted rye germ, fractionation of the extract by ammonium sulfate precipitation, affinity chromatography of the active substances on chitin-beta-glucan and gel filtration on Sephadex G-50. The lectin shows erythroagglutinating activity at a minimum concentration of 2.5 micrograms/ml. The erythroagglutinating activity is the same against human red blood cells of all types of the ABO system and is inhibited by N-acetyl-D-glucosamine. The lectin has no mitogenic activity against mouse splenic lymphocytes. According to the results of polyacrylamide gel electrophoresis the lectin obtained is a mixture of three very similar isolectins of equal erythroagglutinating activity. Sedimentation analysis indicates homogeneity of the lectin preparation; the molecular weight was 56000 as estimated by sedimentation equilibrium. In the presence of urea and sodium dodecyl sulfate the lectin dissociates into 2 types of subunits with molecular weights of 35000 and 19000. The rye germ lectin contains about 2% of neutral sugar and 1% of D-glucosamine. The amino acid composition of the lectin is characterized by a very high content of glycine and half cystine and a low content of apolar amino acids. N-terminal amino acids of the lectin are apparently blocked.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 9","pages":"771-80"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18180633","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}
The kinetic parameters Km and kcat and the proteolytic coefficients kcat/Km for the hydrolysis of eighteen Z(benzyloxycarbonyl)-dipeptide methyl esters with variation of the residues in P1 and P2 position catalyzed by thermitase at pH 8 and 55 degrees C are reported. The results indicate that an integral part of both subsites, S1 and S2, are hydrophobic areas and that a mutual interaction between the side chains of P1 and P2 for optimal hydrolyisis does exist. Furthermore, the importance of the P2 for the peptidolytic activity of thermitase was shown using N-acylated oligo-alanine peptides and their p-nitroanilides. In all cases dialanine or alanine p-nitroanilide are the main products.
{"title":"Investigations on the substrate specificity of thermitase, a thermostable serine-protease from Thermoactinomyces vulgaris.","authors":"U Rothe, D Brömme, A Könnecke, R Kleine","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The kinetic parameters Km and kcat and the proteolytic coefficients kcat/Km for the hydrolysis of eighteen Z(benzyloxycarbonyl)-dipeptide methyl esters with variation of the residues in P1 and P2 position catalyzed by thermitase at pH 8 and 55 degrees C are reported. The results indicate that an integral part of both subsites, S1 and S2, are hydrophobic areas and that a mutual interaction between the side chains of P1 and P2 for optimal hydrolyisis does exist. Furthermore, the importance of the P2 for the peptidolytic activity of thermitase was shown using N-acylated oligo-alanine peptides and their p-nitroanilides. In all cases dialanine or alanine p-nitroanilide are the main products.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 5","pages":"447-50"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17806532","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}
The effect of acetylsalicylic acid (ASA) on tissue sensitivity to insulin was studied in 14 non-obese subjects with impaired glucose tolerance. For the determination of insulin sensitivity a 1 h priming dose-constant insulin infusion technique was used. The percent decrease of plasma glucose and non-esterified fatty acid (NEFA) concentration at comparable steady-state insulin levels was taken as a measure of body sensitivity to insulin. Patients were restudied after daily treatment with 3.0 g ASA over 3 days. The decrease in plasma glucose and NEFA concentration was in the same range prior to and after ASA treatment (20.1 +/- 3.4 vs 20.8 +/- 4.9% and 54.2 +/- 4.8 vs 54.2 +/- 5.4%), indicating no change of insulin sensitivity by ASA treatment. The mean C-peptide concentration during the insulin infusion test did not differ between the two studies. The metabolic clearance rate of insulin was slightly reduced and the disappearance time of insulin was increased after treatment with ASA. In conclusion ASA did not exert any effect on tissue sensitivity to insulin in subjects with impaired glucose tolerance.
本文研究了乙酰水杨酸(ASA)对14例糖耐量受损的非肥胖受试者胰岛素组织敏感性的影响。胰岛素敏感性测定采用1 h引射剂量恒定胰岛素输注技术。在可比较的稳态胰岛素水平下,血浆葡萄糖和非酯化脂肪酸(NEFA)浓度下降百分比作为机体对胰岛素敏感性的量度。每天用3.0 g ASA治疗3天后重新研究患者。ASA治疗前后血浆葡萄糖和NEFA浓度下降幅度相同(20.1 +/- 3.4 vs 20.8 +/- 4.9%, 54.2 +/- 4.8 vs 54.2 +/- 5.4%),说明ASA治疗后胰岛素敏感性未发生变化。胰岛素输注试验期间的平均c肽浓度在两项研究之间没有差异。ASA治疗后胰岛素代谢清除率略有降低,胰岛素消失时间延长。总之,ASA对糖耐量受损的受试者对胰岛素的组织敏感性没有任何影响。
{"title":"Effect of acetylsalicylic acid on insulin sensitivity in subjects with impaired glucose tolerance.","authors":"K P Ratzmann, D Jahr, W Besch, P Heinke, B Schulz","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The effect of acetylsalicylic acid (ASA) on tissue sensitivity to insulin was studied in 14 non-obese subjects with impaired glucose tolerance. For the determination of insulin sensitivity a 1 h priming dose-constant insulin infusion technique was used. The percent decrease of plasma glucose and non-esterified fatty acid (NEFA) concentration at comparable steady-state insulin levels was taken as a measure of body sensitivity to insulin. Patients were restudied after daily treatment with 3.0 g ASA over 3 days. The decrease in plasma glucose and NEFA concentration was in the same range prior to and after ASA treatment (20.1 +/- 3.4 vs 20.8 +/- 4.9% and 54.2 +/- 4.8 vs 54.2 +/- 5.4%), indicating no change of insulin sensitivity by ASA treatment. The mean C-peptide concentration during the insulin infusion test did not differ between the two studies. The metabolic clearance rate of insulin was slightly reduced and the disappearance time of insulin was increased after treatment with ASA. In conclusion ASA did not exert any effect on tissue sensitivity to insulin in subjects with impaired glucose tolerance.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 10","pages":"929-33"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17815705","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":"3rd International Workshop \"Isolated Pancreatic Islets and Diabetes Research.\" Heringsdorf/Usedom, 10-13 May 1982.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 12","pages":"1093-240"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17818077","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}
The probable role of cell surface antigens in the development of juvenile diabetes necessitates a detailed study of the proteins expressed on the surface of pancreatic beta-cells. A gene library composed of genes expressed in beta-cells was constructed to provide a source of low abundance genes from those cells. Initial studies with this library have led to the isolation of three genes which share nucleotide and amino acid sequence homology with mouse and human class I major histocompatibility antigens.
{"title":"Isolation of rat major histocompatibility genes expressed in pancreatic beta-cells.","authors":"W H Kastern, A Lernmark, L Lyngsie","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The probable role of cell surface antigens in the development of juvenile diabetes necessitates a detailed study of the proteins expressed on the surface of pancreatic beta-cells. A gene library composed of genes expressed in beta-cells was constructed to provide a source of low abundance genes from those cells. Initial studies with this library have led to the isolation of three genes which share nucleotide and amino acid sequence homology with mouse and human class I major histocompatibility antigens.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 12","pages":"1135-8"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17818085","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}
The fluorescence of ethidium bromide bound to the DNA of bull spermatozoa can be used for the estimation of intactness and concentration of spermatozoa of washed sperm samples. For the full permeability of the spermatozoal membrane for ethidium bromide digitonin is used in a concentration of 50 micrograms/ml. The fluorescence signals before and after digitonin treatment reflect the portion of cells with intact cellular membrane in the sample. The signal after addition of digitonin correlates to a high degree with the sperm concentration. The method exhibits a sufficient accuracy for the estimation of sperm quality. That applies for the reproducibility with individual ejaculates as well as for the correlation to other methods determining the intactness and sperm concentration. This simple single-step technique requires only about 2 X 10(7) spermatozoa corresponding to 10 to 20 microliters of an average bull ejaculate.
{"title":"A quick test for the simultaneous determination of intactness and concentration of spermatozoa.","authors":"W Halangk, R Bohnensack","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The fluorescence of ethidium bromide bound to the DNA of bull spermatozoa can be used for the estimation of intactness and concentration of spermatozoa of washed sperm samples. For the full permeability of the spermatozoal membrane for ethidium bromide digitonin is used in a concentration of 50 micrograms/ml. The fluorescence signals before and after digitonin treatment reflect the portion of cells with intact cellular membrane in the sample. The signal after addition of digitonin correlates to a high degree with the sperm concentration. The method exhibits a sufficient accuracy for the estimation of sperm quality. That applies for the reproducibility with individual ejaculates as well as for the correlation to other methods determining the intactness and sperm concentration. This simple single-step technique requires only about 2 X 10(7) spermatozoa corresponding to 10 to 20 microliters of an average bull ejaculate.</p>","PeriodicalId":6985,"journal":{"name":"Acta biologica et medica Germanica","volume":"41 10","pages":"899-905"},"PeriodicalIF":0.0,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17943108","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}