{"title":"Differential time course of liver and kidney glucose-6 phosphatase activity during fasting in rats","authors":"Carol Minassian, Gilles Mithieux","doi":"10.1016/0305-0491(94)90146-5","DOIUrl":"10.1016/0305-0491(94)90146-5","url":null,"abstract":"<div><p>We have studied the time course of hepatic and renal microsomal glucose-6 phosphatase (Glc-6Pase) during long-term fasting in the rat. Liver microsomal Glc-6Pase increases up to 48 hr and significantly decreases after 48 hr of fasting. The following activities were determined at 0, 24, 48, 72 and 96 hr: 0.31 ± 0.02; 0.50 ± 0.02; 0.54 ± 0.03; 0.44 ± 0.03; 0.44 ± 0.01 <em>μ</em>mol min<sup>−1</sup> mg protein<sup>−1</sup>, respectively (all values are means ± SEM, <em>n</em> = 6). Concomitantly, kidney microsomal Glc-6Pase progressively increases throughout the fast (<em>V</em><sub>m</sub> = 0.21 ± 0.01; 0.26 ± 0.004; 0.30 ± 0.01; 0.37 ± 0.02; 0.40 ± 0.01 <em>μmol</em><em>min</em><sup>−1</sup> mg protein<sup>−1</sup>, from 0 to 96 hr, respectively). These data suggest that the differential expression of Glc-6Pase activity in the liver and the kidney during long-term fasting could have an important role in the shift from a principally hepatic gluconeogenesis to a hepatic and renal gluconeogenesis.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 99-104"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90146-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18840286","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":"Insect digestive enzymes: properties, compartmentalization and function","authors":"Walter R. Terra, Clélia Ferreira","doi":"10.1016/0305-0491(94)90141-4","DOIUrl":"10.1016/0305-0491(94)90141-4","url":null,"abstract":"","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 1-62"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90141-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88739782","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. Feller, A. Poncin, M. Aittaleb, R. Schyns, Ch. Gerday
{"title":"The blood proteins of the Antarctic icefish Channichthys rhinoceratus: biological significance and purification of the two main components","authors":"G. Feller, A. Poncin, M. Aittaleb, R. Schyns, Ch. Gerday","doi":"10.1016/0305-0491(94)90145-7","DOIUrl":"10.1016/0305-0491(94)90145-7","url":null,"abstract":"<div><p>The lack of hemoglobin and of carbonic anhydrase in the blood of icefish suggest that substantial adaptations of the acid-base balance should occur in order to ensure blood pH homeostasis. The level of peptidic histidyl and of reactive -SH groups per unit of body mass in icefish plasma are 12–13 times higher than those of <em>Notothenia rossii</em>, a common red-blooded Antarctic species. It is proposed that the high level of imidazole ring in icefish plasma improves the non-bicarbonate buffering capacity and that the reactive sulfhydryls are involved in a redox buffer as in some other hypoxia tolerant species. After plasma fractionation on Ultrogel AcA 34, the two main icefish serum proteins have been purified by DEAE cellulose chromatography (IFI) and by HPLC on anion exchange column (IF2). IFI has been identified as a cysteine-rich para-albumin and IF2 as an histidine-rich immunoglobulin-like protein.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 89-97"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90145-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"80097454","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":"Presence of cyclic betaines in fish","authors":"Yuji Ito, Takeshi Suzuki, Takaaki Shirai, Toshiyuki Hirano","doi":"10.1016/0305-0491(94)90148-1","DOIUrl":"10.1016/0305-0491(94)90148-1","url":null,"abstract":"<div><p>The distribution of cyclic betaines were examined comparatively in several organs of 10 species of fish. The distribution of homarine depended on the organs and fish: high levels in gonads, and medium levels in digestive contents and digestive organs were found in Clupeidae and Engraulidae. Homarine was also present in undetected or small amounts in the remaining five species belonging to Plecoglossidae, Scomberesocidae, Carangidae, Sciaenidae and Monacanthidae. Trigonelline and <em>N</em>-methyl isonicotinic acid—isomers of homarine—were scarcely found. Homarine content in fish was not closely related to their food.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 115-124"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90148-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72942306","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}
Huai-Jen Tsai , Su-Ru Shih , Ching-Ming Kuo , Lu-Ku Li
{"title":"Molecular cloning of the common carp (Cyprinus carpio) rhodopsin cDNA","authors":"Huai-Jen Tsai , Su-Ru Shih , Ching-Ming Kuo , Lu-Ku Li","doi":"10.1016/0305-0491(94)90144-9","DOIUrl":"10.1016/0305-0491(94)90144-9","url":null,"abstract":"<div><p>A recombinant phage clone containing a 1584 nucleotides rhodopsin cDNA was screened from a carp retinal cDNA library. The inserted DNA consisting of a single open reading frame of 1062 nucleotides at positions 72 to 1133 encodes a 354 amino acid polypeptide. The deduced amino acid sequence of carp rhodopsin showed 95.7, 85.5 and 74.4% identity with that of goldfish, sand goby and lamprey, respectively. The sites of palmitoylation, glycosylation, disulfide bond formation and Schiff base formation in the putative rhodopsin are all conserved.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 81-88"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90144-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18840287","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}
Sonja Jespersen , Peter Højrup , Svend Olav Andersen , Peter Roepstorff
{"title":"The primary structure of an endocuticular protein from two locust species, Locusta migratoria and Schistocerca gregaria, determined by a combination of mass spectrometry and automatic Edman degradation","authors":"Sonja Jespersen , Peter Højrup , Svend Olav Andersen , Peter Roepstorff","doi":"10.1016/0305-0491(94)90149-X","DOIUrl":"https://doi.org/10.1016/0305-0491(94)90149-X","url":null,"abstract":"<div><p>The complete primary structures of two variants of a protein, Abd-5, isolated from the endocuticles of the migratory locust <em>Locusta migratoria</em> and the desert locust <em>Schistocerca gregaria</em>, have been determined. The proteins from the two species are <em>N</em>-terminally blocked with pyroglutamic acid. Their sequences differed only in two positions. Comparison of the sequences to those of other cuticular proteins shows that moderate homologies exist to 11 other cuticular proteins from insects representing four different orders. Amino acid residues in certain positions appear to be strictly conserved.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 125-138"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90149-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"92071186","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":"Some kinetic properties of amylase from the intestine of the rabbitfish, Siganus canaliculatus (Park)","authors":"Uma Sabapathy, L.H. Teo","doi":"10.1016/0305-0491(94)90150-3","DOIUrl":"10.1016/0305-0491(94)90150-3","url":null,"abstract":"<div><p>The optimum pH of the amylase was 6.5 at 30, 37, 40 and 50°C. At pH 6.5, the amylase had an optimum temperature of 25°C and activation energy (<em>E</em><sub>a</sub>) of 7.3 kcal/mol. The thermostability of the enzyme was determined at 45 and 50°C. The <em>K</em><sub>m</sub> values were determined at various temperatures and found to be lowest at 10 and 50°C and highest at 20°C.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 139-144"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90150-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"88615840","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}
Kee Min Woo , Woelsung Yi , Young Jong Sohn , Chung-Soon Chang , Man-Sik Kang , Doo Bong Ha , Chin Ha Chung
{"title":"Purification and characterization of a poly-l-lysine-activated serine endoprotease from Lumbricus rubellus","authors":"Kee Min Woo , Woelsung Yi , Young Jong Sohn , Chung-Soon Chang , Man-Sik Kang , Doo Bong Ha , Chin Ha Chung","doi":"10.1016/0305-0491(94)90143-0","DOIUrl":"10.1016/0305-0491(94)90143-0","url":null,"abstract":"<div><p>An endoprotease in earthworm (<em>Lumbricus rubellus</em>) is purified to apparent homogeneity using <sup>125</sup>I-lactalbumin as a substrate. The protease has a molecular mass of 27 kDa and is markedly activated by poly-<span>l</span>-lysine or poly-<span>l</span>-arginine. It is a chymotrypsin-like serine protease. Its activity is distributed to coelomic fluid but relatively little to coelomocytes.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 71-80"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90143-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18840285","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}
Elsa Meinardi , Julio M. Azcurra , Monica Florin-Christensen , Jorge Florin-Christensen
{"title":"Coelenterolysin: a hemolytic polypeptide associated with the coelenteric fluid of sea anemones","authors":"Elsa Meinardi , Julio M. Azcurra , Monica Florin-Christensen , Jorge Florin-Christensen","doi":"10.1016/0305-0491(94)90152-X","DOIUrl":"10.1016/0305-0491(94)90152-X","url":null,"abstract":"<div><p>The gastrovascular fluids of the sea anemone <em>Phymactis clematis</em> display strong hemolytic activity, which has basic pH optimum, is thermolabile and is sensitive to proteases. The hemolytic agent from the gastrovascular fluid was partially purified by ammonium sulfate precipitation, chromatography on Dowex-50W cation exchanger and gel filtration on Sephadex G-50. A single peak elutes from the latter with an estimated mol. wt of 18,000. This elution pattern is unaffected if the chromatography is carried out in the presence of 5 M urea. These results indicate that the hemolytic activity is due to a single peptide or a group of peptides of similar size, which we here designate as “coelenterolysin”. Coelenterolysin is also present in sea anemone tissue homogenates, is different from the nematocyst toxin and is not associated with phospholipase activities. It is inhibited by sphingomyelin. This is the first report of hemolytic polypeptides associated with the coelenteric fluid of sea anemones. Coelenterolysin may have a role in extracellular digestion, defense against predators and invasion of the coelenteron by foreign organisms.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 153-161"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90152-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74485577","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}
Luc P. Belzunces, Christophe Lenfant, Sylvie Di Pasquale, Marc-Edouard Colin
{"title":"In vivo and in vitro effects of wheat germ agglutinin and Bowman-Birk soybean trypsin inhibitor, two potential transgene products, on midgut esterase and protease activities from Apis mellifera","authors":"Luc P. Belzunces, Christophe Lenfant, Sylvie Di Pasquale, Marc-Edouard Colin","doi":"10.1016/0305-0491(94)90142-2","DOIUrl":"10.1016/0305-0491(94)90142-2","url":null,"abstract":"<div><p>Wheat germ agglutinin (WGA) and Bowman-Birk soybean trypsin inhibitor represent potential transgene products for inducing pest resistance in plants. The effects of these molecules were studied on midgut esterase and protease activities from <em>Apis mellifera</em> L., a major insect pollinator. Trypsin inhibitor and WGA did not exhibit an acute toxicity in <em>A. mellifera. In vivo</em>, trypsin inhibitor caused a decrease in the amount of trypsin activity and did not have a significant effect on esterase activity. <em>In vitro</em>, trypsin inhibitor inhibited about 80% of non-specific protease activity and 100% of trypsin activity. <em>In vivo</em>, WGA at high concentration in food (1 mg/ml) elicited a large decrease in trypsin activity and did not have a significant effect on esterase activity. <em>In vitro</em>, WGA did not have any significant effect on trypsin and non-specific protease activities but slightly activated esterase activity.</p></div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 63-69"},"PeriodicalIF":0.0,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90142-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"91518385","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}