scholarly journals “Neptune Balls” Polysaccharides: Disentangling the Wiry Seagrass Detritus

Polymers ◽  
2021 ◽  
Vol 13 (24) ◽  
pp. 4285
Author(s):  
Lukas Pfeifer
Keyword(s):  
Mediterranean Region ◽  
World Wide ◽  
Colorimetric Assay ◽  
Posidonia Oceanica ◽  
Land Plant ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Type Analysis ◽  
Selective Precipitation ◽  
Reuse Options

Each year, high amounts of dead seagrass material are washed ashore at beaches world-wide. In the Mediterranean region, the seagrass Posidonia oceanica is responsible for huge agglomerates of ball-like seagrass litter. As these are often removed due to touristic reasons, a reuse method would be a step towards a more ecologically oriented society. In this study, the main polysaccharide components were analyzed, in order to propose possible usage options. To do this, different aqueous fractions were extracted, analyzed by classical carbohydrate analysis methods (GC-FID/MS, colorimetric assay and elemental analysis), and purified by ion-exchange chromatography, as well as selective precipitation with a detecting agent for highly glycosylated glycoproteins. The obtained purified fractions were analyzed in detail and a linkage-type analysis of the most promising extract was conducted via permethylation. Only low amounts of glycoproteins, as well as medium amounts of the characteristic apiogalacturonan were likely to be present, while xylan seemed to be the most abundant polysaccharide in most fractions. A partial structural proposal showed general accordance with land plant xylans, presenting reuse options in the field of biofuel and bioplastic generation.

Clinical Determination of Methemalbumin

1975 ◽  
Vol 21 (10) ◽  
pp. 1506-1510 ◽  
Author(s):  
Scott F Andres ◽  
Thomas J Kregoski ◽  
Charles F Frey ◽  
Ramon R Joseph ◽  
Daisy S McCann
Keyword(s):  
Colorimetric Assay ◽  
Biological Fluids ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Original Sample ◽  
Initial Screening ◽  
Albumin Fraction ◽  
Hemorrhagic Pancreatitis ◽  
Clinical Determination

Abstract We developed an assay for methemalbumin in biological fluids by using diethylaminoethyl-Sephadex ion-exchange chromatography to separate this protein from interfering components, including hemopexin, transferrin, hemoglobin, and haptoglobin/hemoglobin complex. Initial screening of the samples requires measurement of A280/A405 ratios of the peak tubes of the isolated albumin fraction. Values exceeding 30 indicate that methemalbumin is absent, and no further work is required. Values of less than 30 suggest that methemalbumin is present in the original sample, whereupon the presence and amount of methemalbumin can be ascertained by colorimetric assay for iron with use of ferrozine. Results may be expressed either in terms of micrograms of methemalbumin iron per gram of albumin or in milligrams of methemalbumin per liter. The reproducibility of the method is of the order of ±7% (SD). Normal persons have essentially no methemalbumin iron in their serum. Three individuals with hemorrhagic pancreatitis showed values of 65, 98, and 198 µg of methemalbumin Fe per gram of albumin.

Comparison of a Colorimetric Assay for Glycosylated Hemoglobin with Ion-exchange Chromatography

Diabetes ◽  
1979 ◽  
Vol 28 (12) ◽  
pp. 1120-1125 ◽  
Author(s):  
R. E. Pecoraro ◽  
R. J. Graf ◽  
J. B. Halter ◽  
H. Beiter ◽  
D. Porte
Keyword(s):  
Ion Exchange ◽  
Colorimetric Assay ◽  
Glycosylated Hemoglobin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography

scholarly journals Characterization of the antibodies detected by the microscopic agglutination test for bovine leptospirosis

1974 ◽  
Vol 73 (3) ◽  
pp. 425-432 ◽  
Author(s):  
J. A. Morris ◽  
S. N. Hussaini
Keyword(s):  
Ion Exchange ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Agglutination Test ◽  
Microscopic Agglutination Test ◽  
Density Gradient Ultracentrifugation ◽  
Selective Precipitation ◽  
Bovine Leptospirosis

SummaryThe nature of the antibodies detectable by the microscopic agglutination test for bovine leptospirosis was examined. Density gradient ultracentrifugation, gel filtration and disulphide-bond-reduction experiments indicated that antileptospiral agglutinating activity was present in both IgM and IgG immunoglobulin fractions. This was confirmed by selective precipitation of specific antibody classes and ion-exchange chromatography.

Comparison of a colorimetric assay for glycosylated hemoglobin with ion-exchange chromatography

Diabetes ◽  
1979 ◽  
Vol 28 (12) ◽  
pp. 1120-1125 ◽  
Author(s):  
R. E. Pecoraro ◽  
R. J. Graf ◽  
J. B. Halter ◽  
H. Beiter ◽  
D. Porte
Keyword(s):  
Ion Exchange ◽  
Colorimetric Assay ◽  
Glycosylated Hemoglobin ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography

Manual Determination of Intra-Erythrocytic 2,3-Diphosphoglycerate in Whole Blood by Enzymatic Analysis, and Comparison with Ion-Exchange Chromatography

1975 ◽  
Vol 21 (3) ◽  
pp. 376-380 ◽  
Author(s):  
James C Detter ◽  
Donald F Gibson ◽  
Stuart F MacMillan ◽  
Thomas H Oas
Keyword(s):  
Ion Exchange ◽  
Colorimetric Assay ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Single Subject ◽  
Enzymatic Analysis ◽  
Automated Method ◽  
Enzyme Method ◽  
Multiple Samples

Abstract A manual modification of an automated method [Atkinson, K. F., Clin. Chem. 18, 1001 (1972)] for enzymatic assay of 2,3-diphosphoglycerate is described, which is suitable for small laboratories. Samples are easily prepared for analysis, and preparations are stable for several months. Virtually all of the color generated in the colorimetric assay is produced by the diphosphoglycerate-catalyzed reaction. The coefficient of variation for multiple samples from a single subject was 2.4%. Delayed preparation of samples, particularly samples from some acidotic subjects, is shown to result in altered results. The enzyme method is compared with analysis by ion-exchange chromatography.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Preparation and Characterization of NH2-Terminal Fibrinogen Bβ Fragments from N-DSK of Human Fibrinogen

1984 ◽  
Vol 51 (01) ◽  
pp. 016-021 ◽  
Author(s):  
S Birken ◽  
G Agosto ◽  
B Lahiri ◽  
R Canfield
Keyword(s):  
High Performance ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Reverse Phase ◽  
Human Fibrinogen ◽  
Human Volunteers ◽  
Cnbr Cleavage ◽  
Two Peaks

SummaryIn order to investigate the early release of NH2-terminal plasmic fragments from the Bβ chain of fibrinogen, substantial quantities of Bβ 1-42 and Bβ 1-21 are required as immunogens, as radioimmunoassay standards and for infusion into human volunteers to determine the half-lives of these peptides. Towards this end methods that employ selective proteolytic cleavage of these fragments from fibrinogen have been developed. Both the N-DSK fragment, produced by CNBr cleavage of fibrinogen, and Bβ 1-118 were employed as substrates for plasmin with the finding of higher yields from N-DSK. Bβ 1-42 and Bβ 1-21 were purified by gel filtration and ion-exchange chromatography on SP-Sephadex using volatile buffers. When the purified preparation of Bβ 1-42 was chromatographed on reverse-phase high performance liquid chromatography, two peaks of identical amino acid composition were separated, presumably due either to pyroglutamate or to amide differences.

Extracellular polysaccharides from suspension cultures of Nicotiana plumbaginifolia

2020 ◽  
Author(s):  
Ian Sims ◽  
A Bacic
Keyword(s):  
Uronic Acid ◽  
Cell Suspension Cultures ◽  
Anion Exchange Chromatography ◽  
Nicotiana Plumbaginifolia ◽  
Suspension Cultures ◽  
Exchange Chromatography ◽  
Arabinogalactan Protein ◽  
Extracellular Polysaccharides ◽  
Selective Precipitation ◽  
The Individual

The soluble polymers secreted by cell-suspension cultures of Nicotiana plumbaginifolia contained 78% carbohydrate, 6% protein and 4% inorganic material. The extracellular polysaccharides were separated into three fractions by anion-exchange chromatography using a gradient of imidazole-HCl at pH 7 and the individual polysaccharides in each fraction were then isolated by selective precipitation and enzymic treatment. Monosaccharide and linkage compositions were determined for each polysaccharide after reduction of uronic acid residues and the degree of esterification of the various uronic acid residues in each polysaccharide was determined concurrently with the linkage types. Six components were identified: an arabinoxyloglucan (comprising 34% of the total polysaccharide) and a galactoglucomannan (15%) in the unbound neutral fraction, a type II arabinogalactan (an arabinogalactan-protein, 11%) and an acidic xylan (3%) in the first bound fraction, and an arabinoglucuronomannan (11%) and a galacturonan (26%) in the second bound fraction. © 1995.

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