scholarly journals The heparin–protein complex of ox liver capsule. Isolation and chemical characterization

1969 ◽  
Vol 112 (2) ◽  
pp. 167-172 ◽  
Author(s):  
A Serafini-Fracassini ◽  
J J Durward ◽  
L. Floreani
Keyword(s):  
Amino Acid ◽  
Column Chromatography ◽  
Catalytic Hydrogenation ◽  
Protein Complex ◽  
Amino Acid Analysis ◽  
Chemical Characterization ◽  
Isolation And Purification ◽  
Liver Capsule ◽  
Heparin Fractions ◽  
Good Agreement

1. A procedure for the isolation and purification of the heparin–protein complex from ox liver capsule, based on the solubility properties of mucopolysaccharide–cetylpyridinium complexes, is described. 2. The yield of the heparin–protein complex with this method averages 35mg./100g. of dry ox liver capsule. 3. The results of analyses on the polysaccharide show good agreement with values previously published for purified heparin fractions. 4. The amino acid analysis of the protein component shows several similarities to that of chondromucoprotein. 5. The results of β-carbonyl elimination, either with or without catalytic hydrogenation, and column chromatography after β-elimination, show that the polysaccharide is covalently bound to the protein.

scholarly journals The neurotoxins of the sea snake Laticauda schistorhynchus

1983 ◽  
Vol 213 (1) ◽  
pp. 39-41 ◽  
Author(s):  
M L Guinea ◽  
N Tamiya ◽  
H G Cogger
Keyword(s):  
Amino Acid ◽  
Electrophoretic Mobility ◽  
Column Chromatography ◽  
Amino Acid Analysis ◽  
Sea Snake ◽  
Laticauda Semifasciata ◽  
Cellulose Column

Erabutoxins a and b, the major neurotoxins in the venom of the sea snake Laticauda semifasciata, were detected in the venom of Laticauda schistorhynchus. The identity of the toxins was confirmed on the basis of elution position on CM-cellulose column chromatography, disc electrophoretic mobility, amino acid analysis and toxicity measurement.

Preliminary Characterization of Resilin Isolated from the Cockroach, Periplaneta Americana

1992 ◽  
Vol 292 ◽  
Author(s):  
Elizabeth Craig Lombardi ◽  
David L. Kaplan
Keyword(s):  
Mechanical Properties ◽  
Amino Acid ◽  
Amino Acid Analysis ◽  
Periplaneta Americana ◽  
Insect Cuticle ◽  
Oligonucleotide Probes ◽  
Protein Matrix ◽  
Tryptic Fragment ◽  
Good Agreement

AbstractWe would like to mimic the mechanical properties of animal systems for the development of novel materials. Insect cuticle serves as one source of inspiration for the design of these materials. Cuticle is composed of chitin embedded in a protein matrix which may also contain plasticizers, fillers, crosslinkers, and minerals. The specific properties of the cuticle depend on the type, amount and interactions between each component. We are renewing the investigation of the elastic cuticle, resilin. Resilin, a protein-based elastomer first described in the early 1960s, has properties which have been reported to be most like those of ideal rubbers. We have examined resilin isolated from the prealar arms of the cockroach, Periplaneta americana. The results of amino acid analysis are in good agreement with earlier data reported for resilin. A series of tryptic fragments have been isolated and sequenced. These peptides have been used for the design of oligonucleotide probes for the identification of the gene(s) from a teneral cockroach cDNA library. A biopolymer, based on one tryptic fragment, has been designed and synthesized. We are continuing to treat resilin with residue specific proteases in order to map the resilin protein.

Isolation and chemical characterization of outer envelope of Leptospira pomona

1975 ◽  
Vol 21 (7) ◽  
pp. 1102-1112 ◽  
Author(s):  
Joseph A. Zeigler ◽  
William P. VanEseltine
Keyword(s):  
Amino Acid ◽  
Amino Acid Analysis ◽  
Chemical Characterization ◽  
Defined Medium ◽  
Gas Liquid Chromatography ◽  
Outer Envelope ◽  
Intact Cells ◽  
Thin Sections ◽  
Double Track ◽  
Layer Chromatography

Cells of Leptospira interrogans serotype pomona harvested from a chemically defined medium were resuspended in 0.01 M phosphate buffer of pH 7.3. Electron microscopy showed that 90 min of exposure effectively ruptured the outer envelope, freeing it from the cells as small flakes. Both zonal centrifugation in sucrose gradients and centrifugation in isopycnic KBr and CsCl gradients could be used to separate the outer envelope from the axial filaments and protoplasmic cylinders. The latter method resulted in higher yields of purified envelope with the particular protocols used. Thin sections of isolated outer envelope showed the same trilaminar structure seen in sections of intact cells. The outer layers were 1.5 nm thick and appeared as single layers of electron-dense particles. The central electron-transparent layer was 2.0–2.5 nm thick and appeared structureless.The gross chemical composition of the purified outer envelope was 47% protein, 27% carbohydrate, and 23% lipid. Colorimetric carbohydrate determinations revealed hexose, pentose, and 6-deoxyhexose; hexosamine was identified during amino acid analysis. Muramic acid, heptose, and 2-keto-3-deoxyoctonate were not detected. Thin-layer chromatography revealed only polar lipids, about 98% phosphatidylethanolamine and 2% lysophosphatidylethanolamine. Fatty acids identified by gas–liquid chromatography were octadecanoic, octadecenoic, hexadecanoic, and hexadecenoic. Amino acid analysis revealed 17 amino acids, histidine and glutamic acid being most abundant. The outer envelope was interpreted to be comparable with the outer double-track layer found in the cell covering of gram-negative eubacteria.

Capillary electrophoresis and column chromatography in biomedical chiral amino acid analysis

2009 ◽  
Vol 394 (3) ◽  
pp. 695-706 ◽  
Author(s):  
Magdalena C. Waldhier ◽  
Michael A. Gruber ◽  
Katja Dettmer ◽  
Peter J. Oefner
Keyword(s):  
Capillary Electrophoresis ◽  
Amino Acid ◽  
Column Chromatography ◽  
Amino Acid Analysis

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

An ESR study of the peroxidase reaction catalyzed by human methaemoglobin and methaemoglobin-haptoglobin complex

1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček
Keyword(s):  
Hydrogen Peroxide ◽  
Ascorbic Acid ◽  
Amino Acid ◽  
Peroxidase Activity ◽  
Amino Acid Analysis ◽  
Superoxide Radical ◽  
Esr Spectra ◽  
The Other ◽  
Delocalized Electron

The ESR spectra of peroxidase systems of methaemoglobin-ascorbic acid-hydrogen peroxide and methaemoglobin-haptoglobin complex-ascorbic acid-hydrogen peroxide have been measured in the acetate buffer of pH 4.5. For the system with methaemoglobin an asymmetrical signal with g ~ 2 has been observed which is interpreted as the perpendicular region of anisotropic spectrum of superoxide radical. On the other hand, for the system with methaemoglobin-haptoglobin complex the observed signal with g ~ 2 is symmetrical and is interpreted as a signal of delocalized electron. After realization of three repeatedly induced peroxidase processes the ESR signal of the perpendicular part of anisotropic spectrum of superoxide radical is distinctly diminished, whereas the signal of delocalized electron remains practically unchanged. An amino acid analysis of methaemoglobin along with results of the ESR measurements make it possible to derive a hypothesis about the role of haptoglobin in increasing of the peroxidase activity of methaemoglobin.

scholarly journals Isolation and Purification of Fucoxanthin from Brown Seaweed Sargassum horneri Using Open ODS Column Chromatography and Ethanol Precipitation

Molecules ◽  
2021 ◽  
Vol 26 (13) ◽  
pp. 3777
Author(s):  
Yuemei Ye ◽  
Jingwen Sun ◽  
Liting Wang ◽  
Junwang Zhu ◽  
Wei Cui ◽  
...  
Keyword(s):  
Column Chromatography ◽  
Recovery Rate ◽  
Biological Activities ◽  
Brown Seaweed ◽  
Sargassum Horneri ◽  
Scale Production ◽  
Water Mixture ◽  
Isolation And Purification ◽  
Ethanol Precipitation ◽  
Water Solvent

As an abundant marine xanthophyll, fucoxanthin (FX) exhibits a broad range of biological activities. The preparation of high-purity FX is in great demand, however, most of the available methods require organic solvents which cannot meet the green chemistry standard. In the present study, a simple and efficient purification approach for the purification of FX from the brown seaweed Sargassum horneri was carried out. The FX-rich ethanol extract was isolated by octadecylsilyl (ODS) column chromatography using ethanol–water solvent as a gradient eluent. The overwhelming majority of FX was successfully eluted by the ethanol–water mixture (9:1, v/v), with a recovery rate of 95.36%. A parametric study was performed to optimize the aqueous ethanol precipitation process by investigating the effects on the purity and recovery of FX. Under the optimal conditions, the purity of FX was 91.07%, and the recovery rate was 74.98%. Collectively, the eco-friendly method was cost-efficient for the purification of FX. The developed method provides a potential approach for the large-scale production of fucoxanthin from the brown seaweed Sargassum horneri.

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