Bioinorganic chemistry最新文献_第3页

Studies on chelation ofl-DOPA with metal ions and metal-ATP systems dopa与金属离子及金属- atp系统的螯合研究

Bioinorganic chemistry Pub Date : 1978-09-01 DOI: 10.1016/S0006-3061(00)80043-5

K.S. Rajan, S. Mainer, J.M. Davis

{"title":"Studies on chelation ofl-DOPA with metal ions and metal-ATP systems","authors":"K.S. Rajan, S. Mainer, J.M. Davis","doi":"10.1016/S0006-3061(00)80043-5","DOIUrl":"10.1016/S0006-3061(00)80043-5","url":null,"abstract":"<div>The nature and strength of chelation ofl-DOPA with the metal ions, namely, Zn(II), Cu(II), Ni(II), Co(II), Fe(II, III), Mn(II), Ca(II), Mg(II), and Al(III) in both presence and absence of ATP were investigated by thermodynamic equilibrium studies at a constant ionic strength (0.12 M NaCl) and temperature, 25 ± 0.1°C, using the potentiometric pH method. Copper(II), Fe(III), and Al(III) interacted strongly withl-DOPA with the stability constants (logKML, 18.47 ± 0.13, 18.39 ± 0.31, and 19.60 ± 0.20, respectively. In the combined presence of ATP the metal ions were predominantly coordinated with ATP in the pH range 3–5, followed by interaction withl-DOPA above pH = 5 and the formation of the mixed ligand chelates. The stabilities (logKMLA) for the chelation ofl-DOPA with the metal-ATP (1:1) systems varied from 2.32 ± 0.15 to 13.24 ± 0.20 for the different metals. Electronic absorption spectral studies of the metal-l-DOPA systems were undertaken to determine the relative involvement of the different donor groups of the ligand in metal binding. On the basis of the spectral and equilibrium data, the nature and extent of metal binding by the pyrocatechol and the alanine ends of thel-DOPA molecule over the pH range 3–10 are discussed.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"9 3","pages":"Pages 187-203"},"PeriodicalIF":0.0,"publicationDate":"1978-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80043-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90975790","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: 37

Kinetics and Mechanism of Dissociation of Zinc Ion from Carbonic Anhydrase 锌离子与碳酸酐酶解离动力学及机理研究

Bioinorganic chemistry Pub Date : 1978-09-01 DOI: 10.1016/S0006-3061(78)80007-6

Alice Y. Romans, Mary E. Graichen, C.H. Lochmuller, Robert W. Henkens

引用次数: 18

Arsenic and Cancer: Effects of Joint Administration of Arsenite and Selenite on the Genesis of Mammary Adenocarcinoma in Inbred Female C3H/St Mice 砷与癌症:亚砷酸盐和亚硒酸盐联合给药对近交雌性C3H/St小鼠乳腺腺癌发生的影响

Bioinorganic chemistry Pub Date : 1978-09-01 DOI: 10.1016/S0006-3061(78)80005-2

G.N. Schrauzer, D.A. White, J.E. Mcginness, C.J. Schneider, L.J. Bell

引用次数: 49

Binding of platinum to human transferrin 铂与人转铁蛋白的结合

Bioinorganic chemistry Pub Date : 1978-09-01 DOI: 10.1016/S0006-3061(78)80006-4

R. Sterjernholm , F.W. Warner , J.W. Robinson , E. Ezekiel , N. Katayam

引用次数: 12

Modification of cytosine nucleotides: preparation and metalation of a furyl derivative 胞嘧啶核苷酸的修饰:呋喃基衍生物的制备和金属化

Bioinorganic chemistry Pub Date : 1978-09-01 DOI: 10.1016/S0006-3061(00)80044-7

Seth D. Rose, Michael Beer

{"title":"Modification of cytosine nucleotides: preparation and metalation of a furyl derivative","authors":"Seth D. Rose, Michael Beer","doi":"10.1016/S0006-3061(00)80044-7","DOIUrl":"10.1016/S0006-3061(00)80044-7","url":null,"abstract":"<div>O-Furfurylhydroxylamine (FHA) was synthesized and found to react with cytosine derivatives in the presence of sodium bisulfite. Conversion of cytidine to sodiumN4-furfuryloxy-5,6-dihydrocytidine-6-sulfonate by 1 M FHA in aqueous methanolic or ethanolic sodium bisulfite took place with a half-life of 11 min at pH 5 and room temperature. Adenine, guanine, thymine, and uracil derivatives did not react with FHA. The reaction of OsO4/pyridine with a model compound.N6-furfuryadenine (kinetin), resulted in addition of the OsO4 to the furyl group. Calf-thymus DNA and polycytidylic acid were treated with FHA and bisulfite under denaturing conditions. Perchloric acid hydrolysis of the DNA showed that 80% of the cytosines were modified after 1 day. Modification of the cytosine nucleotides in the nucleic acids was followed by treatment with mercuric acetate or osmium tetroxide. The resulting polymers contained three mercury atoms or two osmium atoms per cytosine nucleotide. The potential usefulness of these reactions for electron microscopic studies of nucleic acids is discussed.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"9 3","pages":"Pages 231-243"},"PeriodicalIF":0.0,"publicationDate":"1978-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0006-3061(00)80044-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"84842974","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: 1

Osmium-labeled Polynucleotides: Reaction of Osmium Tetraoxide, with Poly-1,N6-Ethenoadenylic Acid 锇标记的多核苷酸:四氧化锇与聚1,n6 -乙烯腺苷酸的反应

Bioinorganic chemistry Pub Date : 1978-06-01 DOI: 10.1016/0006-3061(78)80006-4

Luigi G. Marzilli, Brian F. Hanson, Leilani Kapili, Seth D. Rose, Michael Beer

引用次数: 3

Bioinorganic chemistry Pub Date : 1978-06-01 DOI: 10.1016/0006-3061(78)80004-0

E. Sabbioni, E. Marafante, L. Amantini, L. Ubertalli, C. Birattari

{"title":"Similarity in metabolic patterns of different chemical species of vanadium in the rat","authors":"E. Sabbioni, E. Marafante, L. Amantini, L. Ubertalli, C. Birattari","doi":"10.1016/0006-3061(78)80004-0","DOIUrl":"10.1016/0006-3061(78)80004-0","url":null,"abstract":"<div>To gain information about the influence of the oxidation state of vanadium on its metabolic behavior, different 48V-labelled vanadium compounds, such as cationic VO2+(V), VO2+(IV), V3+(III), and anionic V4O123−(V), VS43−(V) species were prepared and intravenously injected into rats. The 48V radioactivity was measured in whole tissues as well as in nuclei, mitochondria, lysosomes, microsomes, and cytosols from liver and kidney homogenates. The distribution of 48V redioactivity between the plasma components was investigated using gel filtration of the {48}V-labeled plasma. The findings indicate that there are common pathways of the different chemical forms of vanadium in animals. The similarities are referred to the distribution in different tissues and their intracellular distribution as well as to the transport in the blood, in which 48V was always found in the plasma bound to transferrin. The results obtained tend to exclude a possible influence of the oxidation state of vanadium on its metabolism and support the existence in the body of two mechanisms of conversion of different chemical forms of vanadium ions to one with the same valence.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 6","pages":"Pages 503-515"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3061(78)80004-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11899811","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: 56

Role of Chelation and Water Binding of Calcium in Dormancy and Heat Resistance of Bacterial Endospores 钙螯合和水结合在细菌孢子内休眠和耐热性中的作用

Bioinorganic chemistry Pub Date : 1978-06-01 DOI: 10.1016/0006-3061(78)80002-7

K.S. Rajan, R. Jaw, N. Grecz

{"title":"Role of Chelation and Water Binding of Calcium in Dormancy and Heat Resistance of Bacterial Endospores","authors":"K.S. Rajan, R. Jaw, N. Grecz","doi":"10.1016/0006-3061(78)80002-7","DOIUrl":"10.1016/0006-3061(78)80002-7","url":null,"abstract":"<div>The possible relationship between the water binding by bacterial endospores and their dormancy and heat resistances has been examined in terms of the coordination characteristics of the spore-bound calcium. Stabilities of the calcium complexes of typical cytoplasmic and structural spore components were determined by potentiometric equilibrium pH measurements in model systems consisting of DPA, glycine, alanine, glutamic acid, alanyl-glutamic acid, triglycine, and tetraglycine. The Ca++-form and H+-form spores of Clostridium botulinum 33A were investigated in vivo with respect to their water sorption and heat-resistance characteristics.The results suggest that the complexing of calcium and Ca(II)-DPA may be biologically significant for spore resistance and dormancy at the following three levels: (1) complexing with spore cytoplasmic pool constituents consistent with the idea of a metal-chelate cross-linked cytoplasm or spore cement stabilizing the essential biological macromolecules, (2) complexing with structural components of the spore as indicated by the interaction with model peptides, and (3) coordination with water to produce an apparently dehydrated environment in the spore as evident from the much greater watersorption capacity of the Ca++-form spores vs the much smaller water sorption of the H+-form spores.Interestingly enough, DPA itself, in the absence of metal ion, showed some interaction with di-, tri-, and tetrapeptides and a weak but detectable interaction with amino acids. Although the exact mode of the DPA-peptide interaction is not clear, it is attractive to speculate about its possible involvement in the control of spore dormancy and resistance.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 6","pages":"Pages 477-491"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3061(78)80002-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11568833","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: 9

Autor index 作者索引

Bioinorganic chemistry Pub Date : 1978-06-01 DOI: 10.1016/0006-3061(78)80008-8

引用次数: 0

Kinetics of Formation and Dissociation of Metallocarboxypeptidases 金属羧肽酶的形成和解离动力学

Bioinorganic chemistry Pub Date : 1978-06-01 DOI: 10.1016/0006-3061(78)80001-5

E.J. Billo, K.K. Brito, R.G. Wilkins

{"title":"Kinetics of Formation and Dissociation of Metallocarboxypeptidases","authors":"E.J. Billo, K.K. Brito, R.G. Wilkins","doi":"10.1016/0006-3061(78)80001-5","DOIUrl":"10.1016/0006-3061(78)80001-5","url":null,"abstract":"<div>The rates of formation of a number of metallocarboxypeptidases from metal ions and bovine apocarboxypeptidase A (CPA) have been measured directly and by a competitive method. Rates were determined within pH = 6–8 by utilising the pH change attending metal-ion incorporation, employing indicator and stopped-flow. Second-order rate constants (kf, M−1 s−1 at 25°C, I = 1 M NaCl, pH = 7, Tris = 25 μM) were 1.7 × 105 (Mn2+), 3 × 104 (Co2+), 5 × 103 (Ni2+), 7 × 105 (Zn2+), and 9 × 105 (Cd2+). Relative incorporation rate constants were determined at 25°, pH = 7.0, Tris = 0.1 M, by competing two metal ions for a deficiency of apoprotein and analyzing the products by differential enzyme activity. Agreement between the two methods was reasonable. Rate constants for dissociation of CoCPA, NiCPA, and ZnCPA were measured by loss of enzyme activity on addition of the metal ion scavenger EDTA. Values of kd at 25°, I = 1.0 M NaCl, pH = 7.0 were 8 × 10−3, 3 × 10−5, and 4 × 10−4 s−1, respectively, Values of K obtained kinetically (kf/kd) were in good agreement with those determined by activity measurements of equilibrated solutions. Results are compared with those of bovine apocarbonic anhydrase, where generally significantly slower rates are encountered.</div>","PeriodicalId":9177,"journal":{"name":"Bioinorganic chemistry","volume":"8 6","pages":"Pages 461-475"},"PeriodicalIF":0.0,"publicationDate":"1978-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3061(78)80001-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"11320573","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: 19