Fabrizio Ceciliani , Hugo L. Monaco , Severino Ronchi , Ludovica Faotto , Paola Spadon
{"title":"The primary structure of a basic (pI 9.0) fatty acid-binding protein from liver of Gallus domesticus","authors":"Fabrizio Ceciliani , Hugo L. Monaco , Severino Ronchi , Ludovica Faotto , Paola Spadon","doi":"10.1016/0305-0491(94)90010-8","DOIUrl":"10.1016/0305-0491(94)90010-8","url":null,"abstract":"<div><p>The complete amino acid sequence of a basic (pI 9.0) fatty acid-binding protein purified from liver of <em>Gallus domesticus</em> was determined by automated Edman degradation of tryptic, CNBr/HFBA and <em>Staphylococcus aureus</em> protease peptides. The protein contains 125 amino acid residues which correspond to a molecular mass of 14094. The identification of the blocked <em>N</em>-terminus Ac-Ala required digestion of a SV-8 peptide with the acylamino acid-releasing enzyme prior to sequence analysis. Sequence comparison shows that chicken liver basic-FABP has a significant similarity to other proteins belonging to the superfamily of intracellular lipid molecule binding proteins. Moreover, these sequence data confirm that basic-FABP probably binds its substrate in a slightly different way when compared with other FABPs. Basic-FABP was submitted to the EMBL Data Library with an accession number of P80226</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 261-271"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90010-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18561071","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":"Rates of beta-oxidation of fatty acids of various chain lengths and degrees of unsaturation in highly purified peroxisomes isolated from rat liver","authors":"David S. Chance, Michael K. McIntosh","doi":"10.1016/0305-0491(94)90011-6","DOIUrl":"10.1016/0305-0491(94)90011-6","url":null,"abstract":"<div><p>Highly purified peroxisomes were obtained from the liver of untreated rats, and rates of peroxisomal beta-oxidation were measured using fatty acyl-CoAs differing in chain length and degree of unsaturation. A 20–24-fold purification of peroxisomes, indicated by the specific activities of the marker enzymes catalase and urate oxidase, respectively, was obtained from crude liver homogenate using differential centrifugation techniques followed by a 30% Nycodenz gradient separation. The use of a 30% Nycodenz gradient in the final step of purification was extremely effective (e.g. 5.5-fold reduction) in removing lysosomal contamination. The rate of peroxisomal beta-oxidation with lauroyl-CoA (C12:0) as substrate was the highest of all fatty acyl-CoAs tested. Butyryl-CoA (C4:0) was not oxidized by purified peroxisomes. In general, as chain length of the fatty acyl-CoAs increased above 12 carbons, the rates of beta-oxidation decreased.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 273-280"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90011-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18561072","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":"Kinetic and regulatory properties of pyruvate kinase from Artemia embryos during incubation under aerobic and anoxic conditions. The effect of pH on the kinetic constants","authors":"A. Lazou, A. Frosinis","doi":"10.1016/0305-0491(94)90016-7","DOIUrl":"10.1016/0305-0491(94)90016-7","url":null,"abstract":"<div><p>PK from <em>Artemia</em> embryos displayed sigmoidal kinetics with respect to phosphoenolpyruvate while saturation curves for ADP followed regular hyperbolas. The enzyme was strongly affected by ATP, alanine and fructose 1,6-bisphosphate, the latter increasing the affinity for PEP up to 10-fold. In order to assess whether <em>Artemia</em> PK is regulated by covalent modification, kinetic parameters were determined at various stages of development as well as after exposure of <em>Artemia</em> embryos to anoxic conditions. Incubation under anoxic conditions had no strong effect on the kinetic parameters of the enzyme. In addition, only a small effect of pH changing on the PK kinetic constants was observed. The results of the present study provide no evidence to suggest that <em>Artemia</em> PK is covalently modified in response to anoxia. Therefore, it appears that alternative mechanisms are involved in the depression of metabolic rate observed during the transition of <em>Artemia</em> embryos into anaerobic dormancy.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 325-332"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90016-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86798152","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}
Michael A. Tranulis, Berit Christophersen, Borgar Borrebaek
{"title":"Glucose dehydrogenase in beef (Bos taurus) and rainbow trout (Oncorhynchus mykiss) liver: a comparative study","authors":"Michael A. Tranulis, Berit Christophersen, Borgar Borrebaek","doi":"10.1016/0305-0491(94)90025-6","DOIUrl":"10.1016/0305-0491(94)90025-6","url":null,"abstract":"<div><p>The monomer molecular mass of glucose dehydrogenase (GDH, EC 1.1.1.47) from rainbow trout liver and beef liver were estimated to be 90 kDa for both enzymes, by electrophoresis in the presence of Na-dodecyl-SO<sub>4</sub> (SDS). The 90-kDa proteins were partially degraded to about 60 kDa when purified with a delayed procedure without protease inhibitors. Tryptic cleavage of the 90-kDa proteins gave fragments of about 60 kDa and 30 kDa, being similar for trout and beef GDH. Isoelectric points, kinetic and thermodynamic properties of the two enzymes are markedly different. Triton X-100 stimulated and stabilized the reactions catalysed by the purified enzymes.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 427-435"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90025-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18558303","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}
Laurence Marchat , Philippe M. Loiseau , Christian Poüs , Farrethin Petek
{"title":"Isoenzymatic diagnosis of filariae: a method for separation of lactate dehydrogenase isoenzymes from Molinema dessetae (Nematoda: Filarioidea)","authors":"Laurence Marchat , Philippe M. Loiseau , Christian Poüs , Farrethin Petek","doi":"10.1016/0305-0491(94)90028-0","DOIUrl":"10.1016/0305-0491(94)90028-0","url":null,"abstract":"<div><p>Lactate dehydrogenase (LDH) is highly active in filariae and could be a valuable tool for phyllogeny studies. Unfortunately, the isoenzymatic diagnosis of filariae is often difficult for LDH because of a poor mobility of the enzymes in starch gels which are the most commonly used in such studies. We propose here a method to separate filarial LDH isoenzymes using disc electrophoresis. The experiments were carried out on male and female <em>Molinema dessetae</em> in order to compare their respective isoenzymes. The study of several parameters such as buffer systems, percentage of bisacrylamide and progression time led to optimize the enzyme separation. LDH from male and female filariae were compared to mammal LDH-H4 and LDH-M4. Five and four LDH isoenzymes were found, respectively, in male and female worms. Relative concentration of each isoenzyme diverged between male and female worms. Mammal muscle LDH-M4 type moved between LDH2 and LDH3 from female worms, and between LDH1 and LDH2 from male worms. Mammal heart H4 type enzyme was very different in electrophoretic mobility. The ratio of each isoenzyme was determined by densitometry. The major isoenzymes from female worms will be studied as a biochemical target for chemotherapeutic attack.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 451-457"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90028-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18560841","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}
William W. Christie , Elizabeth Y. Brechany , Ilko N. Marekov , Kamen L. Stefanov , Stoitze N. Andreev
{"title":"The fatty acids of the sponge Hymeniacidon sanguinea from the Black Sea","authors":"William W. Christie , Elizabeth Y. Brechany , Ilko N. Marekov , Kamen L. Stefanov , Stoitze N. Andreev","doi":"10.1016/0305-0491(94)90008-6","DOIUrl":"10.1016/0305-0491(94)90008-6","url":null,"abstract":"<div><p>The fatty acid composition of the sponge <em>Hymeniacidon sanguinea</em> from the Black Sea has been determined by methods involving silver ion HPLC and GC-MS. More than a hundred different fatty acids were identified, of which many were similar to those in sponges from tropical seas. By contrast, some of the fatty acids identified, including <em>trans</em>-6-hexadecenoic acid and 5,15-tetracosadienoic acid, may not have been found previously in sponges and other marine sources, and perhaps are new to science.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 245-252"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90008-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79664380","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":"Nucleotides and the adenylate energy charge as indicators of stress in rainbow trout (Oncorhynchus mykiss) subjected to a range of dissolved oxygen concentrations","authors":"Colleen A. Caldwell, Jeffrey M. Hinshaw","doi":"10.1016/0305-0491(94)90015-9","DOIUrl":"10.1016/0305-0491(94)90015-9","url":null,"abstract":"<div><p>Liver nucleotides (ATP, ADP, AMP, IMP), the adenylate energy charge (AEC), total adenylate concentration (TA), and IMP-load were used as measures of stress in rainbow trout (<em>Oncorhynchus mykiss</em>) acclimated to normoxic (10.0 mg/l), hypoxic (6.5 mg/l), and supersaturated (13.0 mg/l) dissolved oxygen concentrations and subjected to a challenge by confinement. Liver ATP (783.0 nmol/g) was significantly different in the normoxic fish compared to either hyperoxic (447.7 nmol/g) or hypoxic (402.0 nmol/g) fish at the end of the confinement. Within 6.0 hr in the confinement, liver AEC in the normoxic fish increased significantly (0.58) compared to hypoxic (0.42) and hyperoxic fish (0.42). Similarly, the IMP-load in normoxic fish (0.16) decreased to near prestress levels by 6.0 hr in confinement compared to either the hypoxic (0.31) or hyperoxic (0.30) fish. Nucleotides in liver were significantly affected by the dissolved oxygen treatments and the confinement stress in contrast to the muscle nucleotides which were not.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 313-323"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90015-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89579791","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":"Identification of unusual cyclopropane monounsaturated fatty acids from the deep-water lake invertebrate Acanthogammarus grewingkii","authors":"Tomáš Řezanka , Valery M. Dembitsky","doi":"10.1016/0305-0491(94)90023-X","DOIUrl":"10.1016/0305-0491(94)90023-X","url":null,"abstract":"<div><p>In the deep-lake invertebrate, <em>Acanthogammarus grewingkii</em> a number of unusual fatty acids such as <em>cis</em>-11,12-methylene-5-eicosenoate, <em>cis</em>,<em>cis</em>-11,12–14,15-bis-methylene-5-eicosenoate, and their homologues, were identified. The structures were determined from spectra (<sup>1</sup>HNMR, <sup>13</sup>CNMR, mass, IR) after their isolation and quantification by means of Ag<sup>+</sup>-TLC, semipreparative RP-HPLC and capillary GC-MS. The possibility of biosynthesis and function of these unusually fatty acids is discussed, e.g. they may represent a specific feature of animals dwelling in a deep lake or may also be metabolites that are formed in cellular membranes or be of dietary origin.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 407-413"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90023-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85598601","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}
G.D. Engelbrecht , F.H. Van der Bank , P.F.S. Mulder
{"title":"Allozyme variation in Schilbe intermedius Rüppel, 1832 (Pisces, Siluriformes) from the upper Zambezi River System","authors":"G.D. Engelbrecht , F.H. Van der Bank , P.F.S. Mulder","doi":"10.1016/0305-0491(94)90034-5","DOIUrl":"10.1016/0305-0491(94)90034-5","url":null,"abstract":"<div><p>The gene products of 60 protein coding loci in <em>Schilbe intermedius</em> were examined by horizontal starch-gel electrophoresis. Electrophoretic analysis, using muscle and liver tissues, revealed polymorphism at 17 (28.3%) of the loci studied. The average heterozygosity (<em>H</em>) was calculated at 0.029 (±0.009) which is less than values obtained for other fish species. These results suggest that measures should be taken to conserve the genetic variation of this species.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 511-517"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90034-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81150784","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}
Dominique Dorin, Marie-France Sire, Jean-Marie Vernier
{"title":"Demonstration of an antibody response of the anterior kidney following intestinal administration of a soluble protein antigen in trout","authors":"Dominique Dorin, Marie-France Sire, Jean-Marie Vernier","doi":"10.1016/0305-0491(94)90033-7","DOIUrl":"10.1016/0305-0491(94)90033-7","url":null,"abstract":"<div><p>The humoral antibody response following anal intubation of a soluble antigenic protein to trout was investigated. The transfer of human immunoglobulin G (IgGh) to the plasma was demonstrated by ELISA assays. The participation of the anterior kidney in plasma clearance of the antigen was shown by an immunofluorescence study. The anterior kidney displayed a proliferation of specific B lymphocytes and differentiation into plasma cells producing anti-IgGh IgM. The peak of plasma specific antibody concentration occurred 30 days after intubation and a second intubation led to another peak 20 days later, whose amplitude was close to that of the primary response.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 2","pages":"Pages 499-509"},"PeriodicalIF":0.0,"publicationDate":"1994-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90033-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80970436","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}