Hoppe-Seyler's Zeitschrift fur physiologische Chemie最新文献

{"title":"A new metalloproteinase from Pseudomonas fluorescens biotype I.","authors":"P Diermayr,&nbsp;H Klostermeyer","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Isolation and purification of a metalloproteinase from Pseudomonas fluorescens Biotype I are described. The molecular mass of the enzyme is 46 kDa, its isoelectric point is 8.1, its activity is trypsin-like. The amino-acid composition of the single chain protein is given. One molecule of the enzyme contains 1 atom of zinc and 9 atoms of calcium.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 11","pages":"1345-50"},"PeriodicalIF":0.0,"publicationDate":"1984-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17497671","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":"[Intrinsic oxygen affinity: the primary structure of a ruminantia hemoglobin: methionine in betaNA2 of a pecora, the Northern elk (Alces alces alces)].","authors":"H Aschauer,&nbsp;H Wiesner,&nbsp;G Braunitzer","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The primary structures of the alpha- and beta-chains of hemoglobin from the Northern Elk (Alces alces alces) have been determined. The sequence was compared with the bovine chains. The oxygen affinity regarding the primary structure of the beta-chains is discussed.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 11","pages":"1323-30"},"PeriodicalIF":0.0,"publicationDate":"1984-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17567577","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":"[A new peptide alkaloid from Discaria febrifuga Mart].","authors":"R Herzog,&nbsp;A Morel,&nbsp;J Biermann,&nbsp;W Voelter","doi":"10.1515/znb-1984-1236","DOIUrl":"https://doi.org/10.1515/znb-1984-1236","url":null,"abstract":"<p><p>On the basis of spectroscopic investigations (1H-NMR, 13C-NMR, UV, IR and MS spectroscopy), elemental analysis and degradation reactions the structure of a new alkaloid discarine G from the bark extract of Discaria febrifuga Mart. is elucidated.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 11","pages":"1351-4"},"PeriodicalIF":0.0,"publicationDate":"1984-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/znb-1984-1236","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17567578","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":"Interaction of the (2S,3S)-isomer of bestatin with yeast aminopeptidase I. Kinetic and binding studies.","authors":"K H Röhm","doi":"10.1515/bchm2.1984.365.2.1235","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1235","url":null,"abstract":"<p><p>Inhibition of yeast aminopeptidase I by N-[(2S,3S)-3-amino-2-hydroxyl-1-oxo-4-phenylbutyl]-L-leucine [(2S,3S)-Ahp-Leu];a stereoisomer of natural bestatin, is a slow process with half-times in the minute range. Action of the inhibitor is non-competitive with respect to the substrate. Up to 1 mol of (2S,3S)-Ahp-Leu is bound per mol of enzyme subunit. Inhibitor binding does not interfere with binding of essential metal ions but completely suppresses allosteric activation by chloride and high Zn(II)-concentrations. These and other findings suggest that (2S,3S)-Ahp-Leu inhibits aminopeptidase I by stabilizing a weakly active enzyme conformation.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 10","pages":"1235-46"},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1235","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17453969","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":"Tryptophan micro-scale determinations by rapid hydrolysis.","authors":"K Maeda,&nbsp;J J Scheffler,&nbsp;A Tsugita","doi":"10.1515/bchm2.1984.365.2.1183","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1183","url":null,"abstract":"<p><p>A rapid acid-hydrolysis micro method was developed for the accurate determination of the tryptophan contents of proteins. Sample protein (5 micrograms) was hydrolysed in 30 microliters of 3M mercaptoethanesulfonic acid at 166 degrees C for 25 min, resulting in total hydrolysis of the peptide bonds. The subjection of the hydrolysate to an amino-acid analyser revealed the amino-acid composition, including the content of tryptophan with a high recovery of 92%.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 10","pages":"1183-5"},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1183","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17577239","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":"Enhancement of choline dehydrogenase activity in rat liver mitochondria by clofibrate feeding.","authors":"R Kramar,&nbsp;K Kremser,&nbsp;R Raab","doi":"10.1515/bchm2.1984.365.2.1207","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1207","url":null,"abstract":"<p><p>Male rats were fed a diet containing 0.75% clofibrate. After three weeks, the specific activity of choline dehydrogenase of a liver mitochondrial fraction was more then doubled. However, the activity of two other NAD-independent flavoenzymes of the inner mitochondrial membrane namely proline and succinate dehydrogenases were not altered significantly. Thus changes of the inner mitochondrial membrane induced by clofibrate seem to be restricted to some particular enzymes.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 10","pages":"1207-10"},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1207","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17453968","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":"Preferential binding to delta-receptors of the enkephalin-like tetrapeptide Tyr-Ile-Phe-Val. Electrophysiological and conformation studies.","authors":"B Carette,&nbsp;J L Bernier,&nbsp;J P Hénichart","doi":"10.1515/bchm2.1984.365.2.1227","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1227","url":null,"abstract":"<p><p>The technique of microiontophoresis was used to study the effects of leucine-enkephalin [( Leu]enkephalin) and the tetrapeptide Tyr-Ile-Phe-Val on spontaneous and evoked activity of guinea-pig hypothalamic neurons. The inhibitory effects of the tetrapeptide were similar to those of [Leu]enkephalin on some neurons. However, in other cases, [Leu]enkephalin was inhibitory whereas Tyr-Ile-Phe-Val was without effect. These data and the fact that naloxone caused a different antagonism of inhibitory effects by these two peptides suggest the existence of two types of opiate receptors on some hypothalamic neurons and that Tyr-Ile-Phe-Val preferentially binds to delta-receptors. Conformational features of Tyr-Ile-Phe-Val have been established by 1H-NMR spectroscopy and were found to be in accordance with the above considerations. The peptide has a peculiar folded conformation called gamma-turn. Due to the restricted flexibility of this structure, the aromatic moieties (Tyr and Phe) and the hydrophobic (Val) or hydrophilic (terminal NH2 and CO2H) parts are positioned in a specific spatial relationship which can be related to an optimal binding to delta-receptors.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 10","pages":"1227-34"},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1227","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17164425","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":"Carbonate dehydratase (carbonic anhydrase) in a spider. Association with the hemolymph lipoprotein.","authors":"E Stratakis,&nbsp;B Linzen","doi":"10.1515/bchm2.1984.365.2.1187","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1187","url":null,"abstract":"<p><p>Carbonate dehydratase was detected dissolved in the hemolymph of the tarantula, Eurypelma californicum. The enzyme was purified 31-fold by gel filtration, anion-exchange chromatography, a second gel filtration, and finally, preparative polyacrylamide gel electrophoresis. Zinc content increased during purification to up to 2.4 mol Zn/100 000 g of protein (= 1.58 mg Zn/g protein). In the polyacrylamide electrophoresis of tarantula hemolymph under non-denaturing conditions three major protein bands were observed: hemocyanin, a 16 S lipoprotein and the active band which migrated closely behind the 16 S lipoprotein. After treatment with sodium dodecyl sulfate both the carbonate dehydratase-active protein and the lipoprotein revealed bands corresponding to Mr = 95 000 and 110 000, respectively, but the enzymatically active protein revealed an additional third band with Mr = 40 000. The latter band is though to represent the 'true' carbonate dehydratase protein. Upon isoelectric focusing of material containing carbonate dehydratase activity and lipoprotein, bands were obtained at pH 5.45, 5.6 and 5.7. The band at pH 5.6 contained the peak of enzyme activity, and upon dodecyl sulfate-polyacrylamide gel electrophoresis showed the highest proportion of the 40-kDa polypeptide. It is concluded that tarantula carbonate dehydratase, instead of forming a high molecular mass aggregate, is associated with the 16 S lipoprotein, the latter serving as a carrier for the enzyme. The lipoprotein is probably also involved in other transport processes. It is present in great excess and may therefore occur in two forms, charged with carbonate dehydratase or uncharged. Tarantula carbonate dehydratase is inhibited by acetazolamide and by dansylamide, but not by a number of other known inhibitors, most notably not by 4-(aminomethyl)benzenesulfonamide. Treatment with 1M urea does not affect specific enzyme activity, while 2M urea inhibits by 50%. 2-Mercaptoethanol inhibits activity by 50% at 0.1M. Like other carbonate dehydratases, the tarantula enzyme shows esterase activity. The Km for 4-nitrophenyl acetate is 5mM.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 10","pages":"1187-97"},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1187","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17500747","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":"Properties of the arginine esterases from Bitis nasicornis (horned adder) venom.","authors":"F J Joubert,&nbsp;E H Merrifield","doi":"10.1515/bchm2.1984.365.2.1219","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1219","url":null,"abstract":"<p><p>Five forms of arginine esterase (DE-2 to DE-6) were purified from Bitis nasicornis venom by gel filtration on Sephadex G-50, followed by ion exchange chromatography on CM-cellulose and DEAE-sepharose. They contain 17.6 to 23.1% of carbohydrate, 242 to 244 amino acids including 14 half-cystine residues and have molecular masses of about 38 kDa. The enzymes have a high esterolytic activity towards N alpha-benzoyl-L-arginine ethyl ester but show no proteolytic activity against Azocoll and no clotting activity against fibrinogen. Their sequences of the first 19 amino-terminal residues are the same, but their carbohydrate content shows some variation. Furthermore, sequence studies on the N-terminal regions of the arginine esterases from B. nasicornis venom indicate that they share a significant degree of sequence homology with the kallikrein-like enzymes of Crotalus adamanteus and C. atrox venoms and also with porcine pancreatic kallikrein. Studies on tryptic glycopeptides of the arginine esterases show that carbohydrate occurs at the N-terminal region of the molecule and also towards the center.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 10","pages":"1219-25"},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1219","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17627766","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":"Synthesis and opioid activity of [Sar4]dermorphin-tetrapeptide analogues.","authors":"S Salvadori,&nbsp;G Balboni,&nbsp;M Marastoni,&nbsp;G Sarto,&nbsp;R Tomatis","doi":"10.1515/bchm2.1984.365.2.1199","DOIUrl":"https://doi.org/10.1515/bchm2.1984.365.2.1199","url":null,"abstract":"<p><p>The modification of the dermorphin-(1-4)-tetrapeptide structure led to analogues with potent opioid activity in vitro and in vivo. [Sar4]Tetrapeptides such as H2N-CH(NH)-Tyr-D-Ala-Phe-Sar-D-NH-CH(CH3)C6H5 (VII) whose terminal amino group is replaced by the guanidino function and whose C-terminus is amidated by (R)-(+)-alpha-methylbenzylamine, show peripheral and central opioid activities comparable to or higher than those of dermorphin. The potency of VII in the different tests was as follows: guinea-pig ileum (GPI) IC50 = 0.09nM, mouse Vas deferens (MVD) IC50 = 0.69nM, tail-flick ED50 = 8.91 pmol/mouse, i.c.v. and 4.54 mumol/kg, s.c. This dermorphin-(1-4)-tetrapeptide derivative is about 650 and 950 times as active as morphine in the two in vitro tests, respectively. The MVD/GPI potency ratio of the new peptides suggests a mu-type agonist behaviour.</p>","PeriodicalId":13015,"journal":{"name":"Hoppe-Seyler's Zeitschrift fur physiologische Chemie","volume":"365 10","pages":"1199-206"},"PeriodicalIF":0.0,"publicationDate":"1984-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1515/bchm2.1984.365.2.1199","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17151587","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}