Comparative Biochemistry and Physiology Part B: Comparative Biochemistry最新文献

Subcellular localization, metal ion requirement and kinetic properties of arginase from the gill tissue of the bivalve Semele solida 双壳鱼鳃组织精氨酸酶的亚细胞定位、金属离子需求和动力学性质

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90131-7

Nelson Carvajal, Elena Uribe, Claudio Torres

{"title":"Subcellular localization, metal ion requirement and kinetic properties of arginase from the gill tissue of the bivalve Semele solida","authors":"Nelson Carvajal, Elena Uribe, Claudio Torres","doi":"10.1016/0305-0491(94)90131-7","DOIUrl":"10.1016/0305-0491(94)90131-7","url":null,"abstract":"<div>Arginase activity (3.1 ± 0.5 units/g (wet wt) of tissue) was found associated to the cytosolic fraction of the gill cells of the bivalve Semele solida. The enzyme, with a molecular weight of 120,000 ± 3000, was partially purified, and some of the enzymic properties were were examined. The activation of the enzyme by Mn2+ followed hyperbolic kinetics with a KMn value of 0.10 ± 0.02 μM. In addition to Mn2+, the metal ion requirement of the enzyme was satisfied by Ni2+, Cd2+ and Co2+; Zn2+ was inhibitory to ail the Values of Km for arginine and Ki for lysine inhibition, were the same, regardless of the metal ion used to activate the enzyme; Km values were 20 mM at pH 7.5 and 12 mM at the optimum pH of 9.5. Competitive inhibition was caused by ornithine, lysine and proline, whereas branched chain amino acids were non competitive inhibitors of the enzyme.</div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 4","pages":"Pages 683-689"},"PeriodicalIF":0.0,"publicationDate":"1994-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90131-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"90851657","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: 12

Interactions of adenosine triphosphate with snake hemoglobins. Studies in Liophis miliaris, Boa constrictor and Bothrops alternatus 三磷酸腺苷与蛇血红蛋白的相互作用。巨蟒、大蟒蛇和大蟒蛇的研究

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90133-3

Gustavo O. Bonilla , Sérgio Oyama Jr, Cristina L. Nagatomo, Maria S.A. Matsuura, Aldo Focesi Jr

{"title":"Interactions of adenosine triphosphate with snake hemoglobins. Studies in Liophis miliaris, Boa constrictor and Bothrops alternatus","authors":"Gustavo O. Bonilla , Sérgio Oyama Jr, Cristina L. Nagatomo, Maria S.A. Matsuura, Aldo Focesi Jr","doi":"10.1016/0305-0491(94)90133-3","DOIUrl":"10.1016/0305-0491(94)90133-3","url":null,"abstract":"<div>The hemoglobins of three snake species: Liophis miliaris, Bothrops alternatus and Boa constrictor present a single ATP binding site per tetramer. The ATP association constant values for the deoxyhemoglobins at pH 7.5 were about KD ≅ 106 M−1 (107 M−1 for B. contrictor), three to four orders of magnitude higher than the respective values for oxyhemoglobin of about KO ≅ 102 M−1. The deoxyhemoglobin constant values markedly decrease as a function of pH, becoming, at pH 8.5, about KD ≅ 103 M−1 whereas for the oxyhemoglobin the constants remain of about the same, KO ≅ 102 M−1, at the pH range studied. The high ATP binding affinity constants, compared to those of human hemoglobin A, were explained from a molecular structural standpoint, considering L. miliaris hemoglobin, whose complete primary sequence is known. Two distinct amino acid residue differences were found in the β-chain, one being Trp (NA3) (more hydrophobic) in the snake hemoglobin which substitutes the Leu (NA3) in human hemoglobin, and the second being Val 101 β (G3) instead of Glu 101 β (G3). The substitutions could provide an un-neutralized, positively charged, residue Lys-104β and, taking into account its high pK value, the pH dependence of ATP binding affinity for the snake hemoglobin would originate from pH-dependent ionization of phosphate groups of the allosteric effector. The physiological implications of the high ATP binding constant, as well as the possible protective role of the nucleotide binding against the effect of high environmental temperatures on the oxygen dissociation curves, are discussed.</div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 4","pages":"Pages 701-707"},"PeriodicalIF":0.0,"publicationDate":"1994-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90133-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89581487","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

In appreciation 在升值

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90114-7

引用次数: 0

Modification of skeletal muscle sarcoplasmic reticulum fatty acyl composition during arousal from hibernation 冬眠觉醒时骨骼肌肌浆网脂肪酰基组成的改变

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90119-8

Daniel J. Pehowich

引用次数: 10

Comparative biochemistry and physiology B bibliography 比较生物化学与生理学B参考书目

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90138-4

引用次数: 0

Characterization of liver flavin-containing monooxygenase of the dogfish shark (Squalus acanthias) and partial purification of liver flavin-containing monooxygenase of the silky shark (Carcharhinus falciformis) 角鲨(Squalus acanthias)肝脏含黄素单加氧酶的鉴定及丝鲨(Carcharhinus falciformis)肝脏含黄素单加氧酶的部分纯化

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90128-7

Daniel Schlenk, R. Li-Schlenk

{"title":"Characterization of liver flavin-containing monooxygenase of the dogfish shark (Squalus acanthias) and partial purification of liver flavin-containing monooxygenase of the silky shark (Carcharhinus falciformis)","authors":"Daniel Schlenk, R. Li-Schlenk","doi":"10.1016/0305-0491(94)90128-7","DOIUrl":"10.1016/0305-0491(94)90128-7","url":null,"abstract":"<div>Flavin-containing monooxygenase (FMO) activity as N,N-dimethylaniline (DMA) N-oxygenation was characterized in microsomes from the smooth dogfish shark (Squalus acathias). DMA N-oxygenase activity from the liver of the dogfish shark was linear with increasing protein content and over 60 min. The optimal temperature for catalysis was 25°C with a 76 percent reduction in activity when incubated at 15°C and 99 percent loss of activity at 45°C. Optimal pH was approximately 9.6. The maximum velocity for DMA N-oxygenase activity was calculated to be 1.3 nmol min−1 mg−1 with an apparent Michaelis constant of 44 μM. Methimazole oxidase activity was also observed in dogfish liver microsomes which was inhibited by trimethylamine (TMA). Inhibition of DMA N-oxygenase activity by TMA and thiobenzamide was competitive, while inhibition by methimazole was not competitive. Western blot analysis indicated a single liver protein from both Squalus and Carcharhinus of approximately 50 kDa that bound to antibodies raised against FMO 2. An attempt was made to purify FMO as methimazole oxidase from the liver of the silky shark. A single peak of about 10-fold purity was observed following passage through two chromatographic media (CM-Sepharose and HA-Agarose). However, no activity was recoverable after the FMO-containing fractions were applied to a 2′5′ ADP-Sepharose column.</div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 4","pages":"Pages 655-664"},"PeriodicalIF":0.0,"publicationDate":"1994-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90128-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18879978","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: 20

Physicochemical and immunological comparisons between angiotensin I-converting enzymes purified from different mammalian species 从不同哺乳动物中纯化的血管紧张素i转化酶的理化和免疫学比较

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90125-2

Bénédicte Bénéteau-Burnat , Abdelkrim Tahraoui , Frédéric Barbut , Jacqueline Giboudeau , Bruno Baudin

{"title":"Physicochemical and immunological comparisons between angiotensin I-converting enzymes purified from different mammalian species","authors":"Bénédicte Bénéteau-Burnat , Abdelkrim Tahraoui , Frédéric Barbut , Jacqueline Giboudeau , Bruno Baudin","doi":"10.1016/0305-0491(94)90125-2","DOIUrl":"https://doi.org/10.1016/0305-0491(94)90125-2","url":null,"abstract":"<div>Angiotensin I-converting enzyme (ACE) was purified from lungs of pig, rat, monkey and human for comparison of its physicochemical, enzymatic and immunological properties. The protocol involved three chromatographic steps after detergent extraction, i.e. DEAE–Sphérodex ion exchange, lisinopril–Sepharose affinity and Superose 12 HPLC, plus Mono-Q HPLC for monkey ACE. Purified ACE's presented numerous homologies: in particular, closely similar specific activities, catalytic efficiencies, Km's, optimal pH and chloride activations; the molecular weights were about 170 kDa by SDS-PAGE and 320 kDa by gel-filtration on Superose 12; the isoelectric points were about 4.5–4.7. Specific polyclonal antibodies recognized the antigen (porcine ACE) as well as rat, monkey and human ACEs. In contrast, three monoclonal antibodies (F02.4.1, F01.1.3 and F03) produced against porcine ACE showed some differences: they only reacted with pig enzyme and only one (F02.4.1) was anticatalytic. Moreover, the cross-reactivity judged on ELISA with porcine ACE characterized different epitopes specific for the porcine enzyme. In particular, the binding of F02.4.1 was not diminished by previous treatment with saturating concentrations of synthetic competitive ACE inhibitors. Thus, the extrapolation to human of data obtained on animal models should be possible at least for pharmacological and medical trials.</div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 4","pages":"Pages 623-635"},"PeriodicalIF":0.0,"publicationDate":"1994-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90125-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92133879","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: 7

Malate dehydrogenase isozymes in five species of sarcophagid flies (Sarcophagidae: Diptera) 五种石蛉苹果酸脱氢酶同工酶的研究(石蛉科:双翅目)

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90118-X

R.R. Tewari, Sasya Thakur

引用次数: 4

The large subunit of the pig heart mitochondrial membrane-bound β-oxidation complex is a long-chain enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme 猪心脏线粒体膜结合β-氧化复合物的大亚基是长链烯酰辅酶a水合酶:3-羟基酰基辅酶a脱氢酶双功能酶

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90117-1

Song-Yu Yang

{"title":"The large subunit of the pig heart mitochondrial membrane-bound β-oxidation complex is a long-chain enoyl-CoA hydratase: 3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme","authors":"Song-Yu Yang","doi":"10.1016/0305-0491(94)90117-1","DOIUrl":"https://doi.org/10.1016/0305-0491(94)90117-1","url":null,"abstract":"<div>The subunit locations of the component enzymes of the pig heart trifunctional mitochondrial β-oxidation complex are suggested by analyzing the primary structure of the large subunit of this membrane-bound multienzyme complex [Yang S.-Y.et al. (1994) Biochem. biophys. Res. Commun. 198, 431–437] with those of the subunits of the E. coli fatty acid oxidation complex and the corresponding mitochondrial matrix β-oxidation enzymes. Long-chain enoyl-CoA hydratase and long-chain 3-hydroxyacyl-CoA dehydrogenase are located in the amino-terminal and the central regions of the 79 kDa polypeptide, respectively, whereas the long-chain 3-ketoacyl-CoA thiolase is associated with the 46 kDa subunit of this complex. The pig heart mitochondrial bifunctional β-oxidation enzyme is more homologous to the large subunit of the prokaryotic fatty acid oxidation complex than to the peroxisomal trifunctional β-oxidation enzyme. The evolutionary trees of 3-hydroxyacyl-CoA dehydrogenases and enoyl-CoA hydratases suggest that the mitochondrial inner membrane-bound bifunctional β-oxidation enzyme and the corresponding matrix monofunctional β-oxidation enzymes are more remotely related to each other than to their corresponding prokaryotic enzymes, and that the genes of E. coli multifunctional fatty acid oxidation protein and pig heart mitochondrial bifunctional β-oxidation enzyme diverged after the appearance of eukaryotic cells.</div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 4","pages":"Pages 557-566"},"PeriodicalIF":0.0,"publicationDate":"1994-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90117-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92036047","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: 8

Phylogenetic conservation of ganglioside GD3 expression during early vertebrate ontogeny 早期脊椎动物个体发育过程中神经节苷脂GD3表达的系统发育保护

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-12-01 DOI: 10.1016/0305-0491(94)90123-6

R.A. Irvine, T.N. Seyfried

引用次数: 17