scholarly journals The presence of polysaccharide in normal human gastric mucus

1983 ◽  
Vol 215 (2) ◽  
pp. 421-423 ◽  
Author(s):  
J R Clamp ◽  
B Cooper ◽  
J M Creeth ◽  
D Ene ◽  
J Barrett ◽  
...  
Keyword(s):  
Amino Acid ◽  
Molecular Mass ◽  
Density Gradient ◽  
Elemental Analysis ◽  
Density Gradient Ultracentrifugation ◽  
Gastric Mucus ◽  
Average Molecular Mass ◽  
Normal Human ◽  
Beta Elimination

Polysaccharide material was found in the proteolysis glycopolypeptide fraction from normal human gastric mucus. The polysaccharide was identified by carbohydrate and amino acid analyses, by elemental analysis and from its behaviour on density-gradient ultracentrifugation. The polysaccharide is polydisperse with a weight-average molecular mass of 300 000 Da. Over 85% of the polysaccharide consists of galactose, and this represents 26% of all the galactose present in the fractions after beta-elimination with reduction of the glycopolypeptide material.

scholarly journals Isolation of human synovial-fluid hyaluronate by density-gradient ultracentrifugation and evaluation of its protein content

1972 ◽  
Vol 126 (5) ◽  
pp. 1073-1080 ◽  
Author(s):  
Irwin Scher ◽  
David Hamerman
Keyword(s):  
Synovial Fluid ◽  
Density Gradient ◽  
Density Gradient Ultracentrifugation ◽  
Proteolytic Digestion ◽  
Peptide Fragments ◽  
Guanidinium Chloride ◽  
Caesium Chloride ◽  
Normal Human ◽  
Protein Moiety ◽  
Human Synovial Fluid

1. A compound of hyaluronate and protein, called hyaluronate–protein was isolated from pooled human synovial fluids by caesium chloride density-gradient ultracentrifugation. 2. The isolated hyaluronate–protein was labelled with [125I]iodide and the following studies were done. (a) Ultracentrifugation in caesium chloride showed that the protein moiety (125I counts) and hyaluronate (hexuronate) sedimented together in the middle of the gradient. (b) The labelled hyaluronate–protein was treated with trypsin, and ultracentrifugation showed that peptide fragments (125I counts) were dispersed throughout the gradient, indicating proteolytic digestion. Hyaluronate sedimented in the middle of the gradient. (c) The labelled hyaluronate–protein was digested with streptococcal hyaluronidase, and ultracentrifugation showed that hyaluronate fragments were dispersed throughout the gradient, indicating digestion of the polysaccharide. The protein moiety, without attached hyaluronate, now sedimented at the top of the gradient. (d) Ultracentrifugation of labelled hyaluronate–protein in 4m-guanidinium chloride showed that protein and hyaluronate sedimented together. 3. These studies confirm that hyaluronate is combined with a small quantity of protein in normal human synovial fluid. A mild method for the rapid isolation of hyaluronate–protein in good yield is described.

The Binding of Lithium Carmine to a2-Macroglobulin

1969 ◽  
Vol 24 (11) ◽  
pp. 1442-1447 ◽  
Author(s):  
J. J. Picard ◽  
J. F. Heremans
Keyword(s):  
Human Serum ◽  
Density Gradient ◽  
Protein Complex ◽  
Gel Filtration ◽  
Heavy Fraction ◽  
Normal Human Serum ◽  
Density Gradient Ultracentrifugation ◽  
Γ Globulins ◽  
Normal Human

The colloidal dye lithium carmine was added in vitro to normal human serum. Electrophoretic experiments showed that the dye was associated mainly with α2-globulins, small amounts with the albumin and only traces with the γ-globulins. The main complex was eluted with the macroglobulin peak obtained by gel filtration on Sephadex G-200 and sedimented in the heavy fraction on density gradient ultracentrifugation. The dye-protein complex could be precipitated with an antiserum specific for a2-macroglobulin. Gel filtration of a solution of pure a2-macroglobulin, to which lithium carmine was added, demonstrated that the dye was bound to this protein.

scholarly journals The separation and characterization of bronchial glycoproteins by density-gradient methods

1977 ◽  
Vol 167 (3) ◽  
pp. 557-569 ◽  
Author(s):  
J. Michael Creeth ◽  
K. Ramakrishnan Bhaskar ◽  
John R. Horton ◽  
Indrajit Das ◽  
Maria-Teresa Lopez-Vidriero ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Density Gradient ◽  
Acid Composition ◽  
Gradient Methods ◽  
Density Gradient Ultracentrifugation ◽  
Preparative Scale ◽  
Covalent Interaction ◽  
Acetylneuraminic Acid

1. Sputum samples from a total of 18 asthmatic and chronic bronchitic patients were examined by analytical density-gradient ultracentrifugation. CsBr was used as the dispersal agent and dense electrolyte. 2. The patterns show two main groups of components, banding at about 1.3g/ml and 1.5g/ml; in addition, a few samples showed a further zone at approx. 1.65g/ml. These components were identified as protein, secretory glycoprotein and DNA respectively. The glycoprotein zone was frequently hypersharp, and usually contained two or more partially resolved bands; it was always well resolved from the protein. 3. The glycoprotein components were isolated from nine representative sputum samples by density-gradient ultracentrifugation on a preparative scale. Analytical density-gradient ultracentrifugation was used to monitor the efficiency of the separations. 4. Some sputum samples separated cleanly under these conditions, the glycoprotein being essentially devoid of free protein; in others, separation was apparently incomplete, although computer simulation indicated that the conditions were adequate to ensure separation. Further density-gradient separations in CsCl were necessary with several samples before satisfactory products were obtained; mixtures of CsCl with guanidinium chloride were no more effective than CsCl alone. The reluctance to separate indicates a very strong, but non-covalent, interaction between protein and glycoprotein, probably associated with the gelatinous character of the secretion. 5. The purified glycoprotein components were characterized analytically and physicochemically. They contained N-acetylgalactosamine, N-acetylglucosamine, galactose, fucose and N-acetylneuraminic acid, and had an amino acid composition in which serine, threonine and proline predominated; however, aspartic acid, glutamic acid and cystine were also appreciable. The glycoproteins were of very high molecular weight, and usually showed more than one component in sedimentation velocity; their distribution in a density gradient indicated a substantial, but largely monotonic, density heterogeneity. 6. Thiol reduction decreased the molecular weight very substantially, but the products were relatively more homogeneous than the native materials. The amino acid composition was changed significantly and a small and variable proportion of protein or peptide was liberated. It is concluded that the native materials are disulphide-linked aggregates, probably through a cross-linking peptide, in confirmation of earlier studies.

Synthesis of oligotetramethylene oxides with terminal amino groups as curing agents for an epoxyurethane oligomer

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Alexey Slobodinyuk ◽  
Vladimir Strelnikov ◽  
Dmitriy Kiselkov ◽  
Daria Slobodinyuk
Keyword(s):  
High Pressure ◽  
Nmr Spectroscopy ◽  
Ir Spectroscopy ◽  
Molecular Mass ◽  
Elemental Analysis ◽  
Amino Groups ◽  
Average Molecular Mass ◽  
Terminal Amino ◽  
Curing Agents ◽  
C Nmr

Abstract A method for the synthesis of oligotetramethylene oxides with terminal amino groups is presented. Its use as a hardener for urethane-containing oligomers has been demonstrated. The diamines were synthesized by a two-stage method based on oligotetramethylene oxide diol. The compounds can be used for the production of non-toxic, biocompatible and biodegradable segmented urethane-containing elastomers. The oligotetramethylene oxide diol with an average molecular mass of 1008 was chosen as a typical precursor component. Its dibromide was formed using a quasi-phosphonium reagent in various solvents. The corresponding amine was obtained by high-pressure amination. The compounds have been identified by 1H and 13C NMR spectroscopy, IR spectroscopy, and elemental analysis.

Thermus aquaticus ATCC 33923 Amylomaltase Gene Cloning and Expression and Enzyme Characterization: Production of Cycloamylose

1999 ◽  
Vol 65 (3) ◽  
pp. 910-915 ◽  
Author(s):  
Yoshinobu Terada ◽  
Kazutoshi Fujii ◽  
Takeshi Takaha ◽  
Shigetaka Okada
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Molecular Mass ◽  
Minimum Degree ◽  
Cloning And Expression ◽  
Gene Cloning And Expression ◽  
Thermus Aquaticus ◽  
Average Molecular Mass ◽  
Calculated Molecular Mass ◽  
E Coli

ABSTRACT The amylomaltase gene of the thermophilic bacterium Thermus aquaticus ATCC 33923 was cloned and sequenced. The open reading frame of this gene consisted of 1,503 nucleotides and encoded a polypeptide that was 500 amino acids long and had a calculated molecular mass of 57,221 Da. The deduced amino acid sequence of the amylomaltase exhibited a high level of homology with the amino acid sequence of potato disproportionating enzyme (D-enzyme) (41%) but a low level of homology with the amino acid sequence of theEscherichia coli amylomaltase (19%). The amylomaltase gene was overexpressed in E. coli, and the enzyme was purified. This enzyme exhibited maximum activity at 75°C in a 10-min reaction with maltotriose and was stable at temperatures up to 85°C. When the enzyme acted on amylose, it catalyzed an intramolecular transglycosylation (cyclization) reaction which produced cyclic α-1,4-glucan (cycloamylose), like potato D-enzyme. The yield of cycloamylose produced from synthetic amylose with an average molecular mass of 110 kDa was 84%. However, the minimum degree of polymerization (DP) of the cycloamylose produced by T. aquaticus enzyme was 22, whereas the minimum DP of the cycloamylose produced by potato D-enzyme was 17. The T. aquaticus enzyme also catalyzed intermolecular transglycosylation of maltooligosaccharides. A detailed analysis of the activity of T. aquaticus ATCC 33923 amylomaltase with maltooligosaccharides indicated that the catalytic properties of this enzyme differ from those of E. coliamylomaltase and the plant D-enzyme.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

Extraction of polyethylene glycols with dicarbolide solutions in nitrobenzene

1990 ◽  
Vol 55 (8) ◽  
pp. 1959-1967 ◽  
Author(s):  
Petr Vaňura ◽  
Pavel Selucký
Keyword(s):  
Polyethylene Glycol ◽  
Molecular Mass ◽  
Extraction Constant ◽  
Metal Extraction ◽  
Polyethylene Glycols ◽  
Relative Molecular Mass ◽  
Published Data ◽  
Average Molecular Mass ◽  
Peg 400 ◽  
Extraction Constants

The extraction of polyethylene glycol of average molecular mass 400 (PEG 400) with dicarbolide solution in nitrobenzene and of longer-chain polyethylene glycol, of average molecular mass 1 500 (PEG 1 500), with chlorinated dicarbolide solution in nitrobenzene was studied. During the extraction of PEG 400, the polyethylene glycol solvates the Horg+ ion in the organic phase giving rise to the HLorg+ species (L is polyethylene glycol). The obtained value of the extraction constant Kex(HLorg+) = 933 is consistent with published data of metal extraction. Extraction of PEG 1 500 was treated applying the simplified assumption that the thermodynamic behaviour of PEG 1 500 is the same as that of n molecules of polyethylene glycol with relative molecular mass 1 500/n, each solvating one cation. For this model, the value of n = 3.2 ± 1.1 and the values of the extraction constants of the HL1/n,org+ and HL2/n,org+ species were obtained by using the adapted program LETAGROP. This value of n is consistent with published extraction data in the presence of polyethylene glycol with a relative molecular mass from 200 to 1 000.

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