Bioinorganic chemistry最新文献_第10页

Copper metabolism in the rat: effects of copper loading and copper depletion 大鼠铜代谢:铜负荷和铜耗竭的影响

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80151-9

V. Albergoni, N. Favero, G.P. Rocco

引用次数: 7

Characterization of nickel(II) bovine carbonic anhydrase and its inhibitor derivatives 镍(II)牛碳酸酐酶及其抑制剂衍生物的表征

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80133-7

I. Bertini, E. Borghi, C. Luchinat

引用次数: 12

Author index to volume 9 第九卷的作者索引

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80139-8

引用次数: 0

Formation and spectral characterization of Cu(II)-Poly(L-Ornithine) complexes Cu(II)-聚(l -鸟氨酸)配合物的形成和光谱表征

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80002-2

Canh-Vang Phan Lucia Tosi, Arlette Garnier

引用次数: 16

Complexes of cobalt (II) and manganese (II) with adenosine 5′-diphosphate and adenosine 5′-triphosphate. A circular dichroism study 钴(II)和锰(II)与5′-二磷酸腺苷和5′-三磷酸腺苷的配合物。圆二色性研究

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80195-7

Jacques Bolard, Genevieve Chottard

{"title":"Complexes of cobalt (II) and manganese (II) with adenosine 5′-diphosphate and adenosine 5′-triphosphate. A circular dichroism study","authors":"Jacques Bolard, Genevieve Chottard","doi":"10.1016/S0006-3061(00)80195-7","DOIUrl":"10.1016/S0006-3061(00)80195-7","url":null,"abstract":"<div>For studies of interactions between Co2+ and adenosine 5′-diphosphate or adenosine 5′-triphosphate (ADPH4+ and ATPH5+ in strongly acidic medium) visible circular dichroism (d-d transitions of Co2+) and ultraviolet circular dichroism (adenine transitions) have proven to be very sensitive to structural changes. Drastic variation of spectra as a function of pH and concentration enabled us to show the existence of various species, to state their stoichiometry and eventually, their self-association. With ATPH22-, C.D. results are in agreement with recent N.M.R. results. With ligands bearing three negative charges, complexes (1 metal:2 nucleotides)n are formed in which bases of the two nucleotides of the molecule are self-associated. With ADP3-, the visible C.D. spectrum of this complex is intense and hides the spectra of the complexes formed with other protonated species of ADP; this self-associated complex is detected up to a lower limit of 5 × 10-4 M concentration. With ATPH3-, a complex exhibiting the same characteristics as the one with ADP3- is formed but in about twenty times less amount which explains why it was not detected by potentiometry. With 0.1 M ATP4-, dimeric (or polymeric) complexes, of 1:2 and 1:1 stoichiometry are observed. With 0.01 M ATP4-, 1:1 monomeric and 2:1 dimeric (or polymeric) complexes are detected. The interactions between Mn2+ ions and ADP or ATP have been studied by C.D. on the UV range. The same species as with CO2+ ions have been found but the 1:2 complex formation with ADP3- was shown to occur to a lesser exten and was not observed below a 10-2 M ADP concentration.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 3","pages":"Pages 215-224"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80195-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11249282","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: 5

Selenium proteins in ovine tissues: III distribution of selenium and glutathione peroxidases in tissue cytosols 羊组织中的硒蛋白:III硒和谷胱甘肽过氧化物酶在组织细胞质中的分布

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80241-0

R.S. Black, M.J. Tripp, P.D. Whanger, P.H. Weswig

{"title":"Selenium proteins in ovine tissues: III distribution of selenium and glutathione peroxidases in tissue cytosols","authors":"R.S. Black, M.J. Tripp, P.D. Whanger, P.H. Weswig","doi":"10.1016/S0006-3061(00)80241-0","DOIUrl":"10.1016/S0006-3061(00)80241-0","url":null,"abstract":"<div>Three 6 week-old lambs were injected with carrier-free selenium-75 as sodium selenite initially and again after 6 days. One lamb received no further injections whereas the other two received injections of either vitamin E or unlabeled Na2SeO3 when the first selenium-75 injection was given. Selected tissues were removed at autopsy 10 days after the first injection. The cytosol from homogenates of these tissues was subjected to gel chromatography, and the elution profiles determined for radioactivity, protein content, and glutathione peroxidase activity using either hydrogen peroxide or cumene hydroperoxide as substrates. The selenium-75 was found to be distributed mainly between 2 different MW peaks. The larger MW seleno-peak (90,000) possessed both glutathione:hydrogen peroxide oxidoreductase, and glutathione:cumene hydroperoxide oxidoreductase activities, but the smaller MW seleno-peak (about 10,000) possessed no glutathione peroxidase activity. A peak of about 60,000 daltons containing only glutathione:cumene hydroperoxide oxido-reductase activity and no selenium-75 was found primarily in the liver and kidney. Vitamin E had no effect on the elution profiles. Selenium status of the animal had only a minor effect on the selenium-75 distribution in the cytosol, but had a marked effect on the absolute amount of label taken up by tissues.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 2","pages":"Pages 161-172"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80241-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11841961","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: 44

Selenium in human nutrition: Dietary intakes and effects of supplementation 人体营养中的硒:膳食摄入量和补充效果

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80164-7

G.N. Schrauzer, D.A. White

{"title":"Selenium in human nutrition: Dietary intakes and effects of supplementation","authors":"G.N. Schrauzer, D.A. White","doi":"10.1016/S0006-3061(00)80164-7","DOIUrl":"10.1016/S0006-3061(00)80164-7","url":null,"abstract":"<div>The dietary selenium intakes of a young couple residing in Southern California were determined to be 107 and 99 μgrams/day for the husband and the wife, respectively, on the basis of a 30 day study. For other young adult Californians, the selenium intakes were estimated from 90 to 168 μgrams/day. The highest intakes were observed in individuals subsisting on diets rich in whole wheat grain cereal products and seafoods. The selenium concentrations in whole blood of the subjects under study correlated with the dietary selenium intakes directly (P<0.001). The administration of 150 μgrams of selenium/day in the form of commercially available supplements increases the blood selenium concentrations. After 3 weeks of supplementation, the selenium concentrations in whole blood of our subjects reached 0.21 μgrams/ml. Prolonged supplementation at higher Se dosage levels causes further increases of the blood concentrations: Two individuals who had been ingesting 350 and 600 μgrams/day for 18 months exhibited blood selenium levels of 0.35 and 0.62 μgrams/ml. The blood selenium concentration of all subjects declined slowly after cessation of supplementation. Selenium uptake from the supplements was not affected by the joint administration of zinc supplements at 15 mg zinc/day. Glutathione peroxidase blood levels did not correlate with blood Se concentrations.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 4","pages":"Pages 303-318"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80164-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11849057","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: 156

Interactions of Cis- and Trans-platinum(II) complexes with dehydrogenase enzymes in the presence of different mono- and polynucleotides: Evidence for a ternary complex 顺式和反式铂(II)配合物在不同单核苷酸和多核苷酸存在下与脱氢酶的相互作用:三元配合物的证据

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80167-2

Michael E. Friedman, Paul Melius, John E. Teggins, Charles A. McAuliffe

{"title":"Interactions of Cis- and Trans-platinum(II) complexes with dehydrogenase enzymes in the presence of different mono- and polynucleotides: Evidence for a ternary complex","authors":"Michael E. Friedman, Paul Melius, John E. Teggins, Charles A. McAuliffe","doi":"10.1016/S0006-3061(00)80167-2","DOIUrl":"10.1016/S0006-3061(00)80167-2","url":null,"abstract":"<div>The inhibition of several dehydrogenase enzymes by cis- and trans- Pt(NH3)2Cl2 have been measured in the presence of baker yeast ribonucleic acid (RNA), calf thymus and salmon sperm deoxyribonuclic acid (DNA) and several mononucleotides (AMP and ATP). The binding constants for the interaction of the platinum complexes to the nucleotides have been calculated and a comparison of those values to the previously calculated platinum complex-enzyme binding constants strongly suggest that platinum compounds are more tightly bound to the enzymes. The binding of the platinum complexes to most of the enzymes was decreased in the presence of any nucleotide, yet it was observed that when using rabbit muscle (M4) lactate dehydrogenase the mononucleotides reduced the binding to a lesser degree while the polynucleotides actually enhanced the platinum-enzyme interaction. The implications of these interactions are discussed.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 4","pages":"Pages 341-353"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80167-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11849058","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: 10

A fluorescence study of the binding of calcium and terbium ions to angiotensin 钙和铽离子与血管紧张素结合的荧光研究

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80169-6

Robert E. Lenkinski , Jerry D. Glickson , Roderich Walter

引用次数: 11

A light-scattering study of the effect of calcium chloride on the molecular weight of busycon hemocyanin 氯化钙对水仙桃血青素分子量影响的光散射研究

Bioinorganic chemistry Pub Date : 1978-01-01 DOI: 10.1016/S0006-3061(00)80239-2

M.Constance Loeffler, Shian-shi Su, Norman C. Li, Edward F. Casassa

{"title":"A light-scattering study of the effect of calcium chloride on the molecular weight of busycon hemocyanin","authors":"M.Constance Loeffler, Shian-shi Su, Norman C. Li, Edward F. Casassa","doi":"10.1016/S0006-3061(00)80239-2","DOIUrl":"10.1016/S0006-3061(00)80239-2","url":null,"abstract":"<div>Solutions of Busycon canaliculatum have been studied by light scattering. In 0.05 M Trizma buffer + 0.1 M NaCl at pH 7.0 at 14°, the weight-average molecular weight is 8.9 X 106. In the presence of added CaCl2 (0.02 M), the molecular weight of the protein increases to 10.7 X 106, and the second virial coefficient is reduced. At pH 9.95, the molecular weights with and without 0.02 M CaCl2, are 3.7 X 106 and 1.3 X 106, respectively; and the effect of Ca++ in reducing the second virial coefficient is much greater than at pH 7.0. These results can be understood on the basis that at pH 7.0, Ca++ increases the association of hemocyanin, by binding and intermolecular linkage through the carboxyl groups of protein side chains. At pH 9.95, amino groups are deprotonated and therefore also become available for Ca++ binding. The relative effect of Ca++ in enhancing the association of hemocyanin therefore becomes greater at the higher pH.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 2","pages":"Pages 133-138"},"PeriodicalIF":0.0,"publicationDate":"1978-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80239-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11248008","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