Hoppe-Seyler's Zeitschrift fur physiologische Chemie最新文献_第10页

Isozyme pattern of thymidine kinase during liver regeneration. 肝脏再生过程中胸苷激酶同工酶谱。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.457

J Coloma, J V Castell

引用次数: 7

Synthesis of the C-terminal undeca- and protected docosapeptide of bovine insulin B-chain. 牛胰岛素b链c端未解肽和受保护肽的合成。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.485

B Hemmasi, W Stüber, E Bayer

引用次数: 1

Cigarette smoke components are not very effective in directly inactivating alpha 1-proteinase inhibitor. 香烟烟雾成分对直接灭活α-1-蛋白酶抑制剂的作用不大。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.511

A Wyss, G D Virca, H P Schnebli

引用次数: 6

Immunochemical analysis of substance P using its synthetic fragments and analogs. P物质合成片段和类似物的免疫化学分析。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.499

C S Cierniewski, A Babińska, W Koziołkiewicz, T Wasiak

引用次数: 2

Isolation and characterization of an oligosaccharide- and glycoprotein-specific sialidase from human leucocytes. 人白细胞低聚糖和糖蛋白特异性唾液酸酶的分离和鉴定。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.419

R Schauer, M Wember, H Tschesche

引用次数: 22

On the mechanism of lactate dehydrogenase leakage from normal and D-galactosamine-treated hepatocytes in monolayer culture. 单层培养正常和d -半乳糖胺处理的肝细胞乳酸脱氢酶渗漏的机制。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.427

A Eisenmann, J E Phillips, A Schulze-Specking, K Decker

{"title":"On the mechanism of lactate dehydrogenase leakage from normal and D-galactosamine-treated hepatocytes in monolayer culture.","authors":"A Eisenmann, J E Phillips, A Schulze-Specking, K Decker","doi":"10.1515/bchm2.1984.365.1.427","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.1.427","url":null,"abstract":"Synthesis, degradation and leakage of lactate dehydrogenase and of total protein was measured using D-galactosamine-treated rat hepatocytes in monolayer culture. The kinetics of [3H]leucine incorporation into trichloroacetic acid-precipitable material and into isolated lactate dehydrogenase of cells and of the extra-cellular space revealed a similar extent of inhibition of both synthesis and leakage following exposure to D-galactosamine. Hepatocyte cultures that had been labeled before D-galactosamine treatment lost intracellular protein-associated radioactivity almost as rapidly as control cells up to the time of measurable enzyme leakage; thereafter, the rate of 3H-loss increased in the treated cells. Lactate dehydrogenase present in the medium is degraded less rapidly than the enzyme in the intracellular space. This explains the apparent increase of total lactate dehydrogenase activity in D-galactosamine-treated as compared to control cultures. Following [3H]leucine addition to D-galactosamine-treated cultures, the specific radioactivity of the leaked lactate dehydrogenase in the medium was never greater than that of the enzyme in the cytosolic compartment. The data rule out a direct excretion of newly synthesized enzyme as a result of D-galactosamine action.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 4","pages":"427-36"},"PeriodicalIF":0.0,"publicationDate":"1984-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.1.427","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17788615","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}

引用次数: 6

The amino-acid sequence of alpha A- and beta-chains from the major hemoglobin component of American flamingo (Phoenicopterus ruber ruber). 美洲火烈鸟(Phoenicopterus ruber ruber)血红蛋白主要成分α - A-和β -链的氨基酸序列。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.437

J Godovac-Zimmermann, G Braunitzer

引用次数: 12

The isolation of tetrahydroxy bile acids as methyl esters from human urine and their characterization by 1H- and 13C-nuclear magnetic resonance spectroscopy. 以甲酯形式从人尿中分离四羟基胆汁酸，并用1H-和13c核磁共振波谱对其进行表征。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.479

P Back, H Fritz, C Populoh

引用次数: 20

Interaction of Vicia graminea anti-N lectin with cell surface glycoproteins from erythrocytes with rare blood group antigens. 小麦抗n凝集素与罕见血型抗原红细胞表面糖蛋白的相互作用。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.469

D Blanchard, A Asseraf, M J Prigent, J J Moulds, D Chandanayingyong, J P Cartron

{"title":"Interaction of Vicia graminea anti-N lectin with cell surface glycoproteins from erythrocytes with rare blood group antigens.","authors":"D Blanchard, A Asseraf, M J Prigent, J J Moulds, D Chandanayingyong, J P Cartron","doi":"10.1515/bchm2.1984.365.1.469","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.1.469","url":null,"abstract":"The erythrocyte receptors for Vicia graminea (Vg) anti-N lectin have been investigated after 125I-labelling of the purified lectin and binding to membrane components separated by dodecyl sulphate polyacrylamide gel electrophoresis. GP alpha (synonym glycophorin A or MN glycoprotein) and GP delta (synonym glycophorin B or Ss glycoprotein) are the main Vg receptors of native human blood group NN and MN erythrocytes whereas Vg lectin only binds to GP delta from MM red cells. The glycoprotein of 28 kDa present in Mi III erythrocytes (a presumed variant of GP delta) carries Vg receptors. Both binding studies and agglutination experiments with this lectin suggest that the delta Mi III gene might produce more glycoprotein molecules than the normal delta gene. Binding of Vg lectin to hybrid glycoproteins [from Mi V, St(a+) and Dantu (+) donors] produced by unequal crossing-over between alpha and delta genes, may occur if the molecules exhibit N activity. The lectin does not bind to sialic acid- and galactose-deficient glycoproteins from Tn erythrocytes and no binding could be detected in the region of GP delta of erythrocytes from S-s-U-individuals. Addition of N-acetylgalactosamine residues to the alkali-labile oligosaccharides attached to GP alpha and GP delta, as found in Cad erythrocytes, decrease the binding capacity for Vg lectin. Finally the absence of Vg lectin binding sites on native GP alpha molecule from MgMg and McM erythrocytes, which carry well defined variants of this glycoprotein, supports the view that the binding site of the lectin on native glycoproteins is located at the N-terminal end of glycoprotein (GP alpha and GP delta) with N specificity (N-terminus = Leu).","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 4","pages":"469-78"},"PeriodicalIF":0.0,"publicationDate":"1984-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.1.469","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17788598","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}

引用次数: 15

Sialidase assay by luminescence in the low picomole-range of sialic acid. Its application to the measurement of this activity in influenza virus. 发光法测定唾液酸低皮摩尔范围的唾液酸酶。应用于流感病毒中这种活性的测定。

Hoppe-Seyler's Zeitschrift fur physiologische Chemie Pub Date : 1984-04-01 DOI: 10.1515/bchm2.1984.365.1.415

J A Cabezas, N Pérez, M Llanillo, A Reglero, P Calvo

{"title":"Sialidase assay by luminescence in the low picomole-range of sialic acid. Its application to the measurement of this activity in influenza virus.","authors":"J A Cabezas, N Pérez, M Llanillo, A Reglero, P Calvo","doi":"10.1515/bchm2.1984.365.1.415","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.1.415","url":null,"abstract":"A new procedure for a sialidase assay, by bioluminescence, has been developed. The substrate, N- acetylneuraminyllactose (sialyllactose), hydrolysed by the sialidase activity, releases lactose. This lactose is hydrolysed with beta-galactosidase. The released galactose is oxidized with galactose dehydrogenase and NAD. The NADH produced in the last step is measured by a luminescence system, coupling two enzymes, NAD(P)H dehydrogenase (FMN) and luciferase. This microassay, which is specific, rapid, simple and ultra-sensitive, is a measure for amounts as little as (at least) 5 pmol of N-acetylneuraminic acid (corresponding to 0.15 ng of the released sialic acid). It uses commercialized reagents (non-radioisotopic) and avoids interferences common in other procedures. This method has been used for measuring sialidase activity directly on intact virus, avoiding inconvenient modifications produced in the extraction of the enzyme. The specific activity of sialidase of influenza virus X31 (H3N2), determined by this procedure, is 0.65 U/mg of total virus protein.","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 4","pages":"415-8"},"PeriodicalIF":0.0,"publicationDate":"1984-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.1.415","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17788613","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}

引用次数: 4