scholarly journals THE NUMBER OF POLYPEPTIDE CHAINS IN BOVINE PLASMA ALBUMIN

1956 ◽  
Vol 34 (2) ◽  
pp. 160-169 ◽  
Author(s):  
M. E. Reichmann ◽  
J. Ross Colvin
Keyword(s):  
Molecular Weight ◽  
Light Scattering ◽  
Sodium Chloride ◽  
Sedimentation Velocity ◽  
Performic Acid ◽  
Sedimentation Equilibrium ◽  
Plasma Albumin ◽  
Disulphide Bonds ◽  
Bovine Plasma ◽  
Polypeptide Chains

The molecular weight of performic acid oxidized bovine plasma albumin, dispersed in 0.08 M borate +0.2 M sodium chloride buffer, pH 7.4, was estimated as 30,000 by light-scattering and sedimentation equilibrium methods, 19,000 by osmotic pressure. Sedimentation velocity analyses and electrophoresis showed that the component polypeptide chains of the material are similar in mass and charge density so the polydispersity must be attributed to labile aggregates. The results indicate that here are at least three and probably four similar polypeptide chains in the molecule of native bovine plasma albumin, held together by disulphide bonds.

MOLECULAR WEIGHT OF BOVINE PLASMA ALBUMIN, VITELLENIN, AND THEIR OXIDATION PRODUCTS IN FORMIC ACID

1961 ◽  
Vol 39 (9) ◽  
pp. 1405-1417 ◽  
Author(s):  
W. G. Martin
Keyword(s):  
Molecular Weight ◽  
Formic Acid ◽  
Transient State ◽  
Oxidation Products ◽  
Performic Acid ◽  
Bond Rupture ◽  
Acid Oxidation ◽  
Plasma Albumin ◽  
Viscosity Measurements ◽  
Bovine Plasma

Sedimentation, diffusion, and Archibald transient state measurements were made on bovine plasma albumin and vitellenin of egg yolk in formic acid (88% w/w) solution. The molecular weight of bovine plasma albumin, averaging 77 × 103and 70 × 103with and without added salt, respectively, indicated that peptide bonds were stable to the acid for at least 1 week (storage at 5 °C and measurement periods at 20 °C). Similar values were obtained from estimates based on viscosity measurements but greater deviations occurred. Vitellenin had a mean molecular weight of 93 × 103from sedimentation and diffusion but polydispersity was revealed by the Archibald measurements (molecular weights from 55 × 103to 10 × 103). Higher values of molecular weight were obtained for vitellenin by varying the dissolution technique and exposure time in formic acid and also when viscosity measurements were used to compute molecular weight. Analyses of N-terminal amino acids showed that peptide bond rupture was not a major factor in the polydispersity of vitellenin. Although aggregates are probably present in formic acid solutions of this protein, it appears to be naturally polydisperse. Both albumin and vitellenin were considerably degraded by performic acid oxidation procedures.

scholarly journals Purification and properties of 6-phosphogluconate dehydrogenase from sheep liver

1969 ◽  
Vol 115 (4) ◽  
pp. 639-643 ◽  
Author(s):  
R. H. Villet ◽  
K. Dalziel
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sedimentation Velocity ◽  
Sedimentation Equilibrium ◽  
Equilibrium Studies ◽  
Phosphogluconate Dehydrogenase ◽  
Sheep Liver ◽  
Equilibrium Sedimentation ◽  
Purification And Properties

A method is described for the isolation of 6-phosphogluconate dehydrogenase from sheep liver. The product appears to be homogeneous in polyacrylamide-gel electrophoresis and in sedimentation-velocity and sedimentation-equilibrium studies in the ultracentrifuge. The molecular weight is estimated as 129000 from equilibrium sedimentation.

Light-scattering study of the effect of sodium chloride on the molecular weight of human adult hemoglobin

Biochemistry ◽  
1971 ◽  
Vol 10 (17) ◽  
pp. 3222-3229 ◽  
Author(s):  
Chien Ho ◽  
Ingrid B. E. Noren ◽  
Edward F. Casassa
Keyword(s):  
Molecular Weight ◽  
Light Scattering ◽  
Sodium Chloride ◽  
Human Adult ◽  
Adult Hemoglobin ◽  
Scattering Study

scholarly journals Molecular weights of the Thy-1 glycoproteins from rat thymus and brain in the presence and absence of deoxycholate

1978 ◽  
Vol 169 (2) ◽  
pp. 411-417 ◽  
Author(s):  
P W Kuchel ◽  
D G Campbell ◽  
A N Barclay ◽  
A F Williams
Keyword(s):  
Molecular Weight ◽  
Equilibrium Dialysis ◽  
Sedimentation Coefficient ◽  
Sedimentation Equilibrium ◽  
Membrane Glycoproteins ◽  
Guanidinium Chloride ◽  
Molecular Weights ◽  
Methionine Residue ◽  
Disulphide Bonds ◽  
Binding Data

1. The Thy-1 membrane glycoproteins from rat thymus and brain bound deoxycholate to 24% of their own weight as measured by equilibrium dialysis. The binding occurred co-operatively at the critical micelle concentration of deoxycholate, suggesting that the glycoproteins bind to a micelle, and not to the detergent monomer. 2. From sedimentation-equilibrium and deoxycholate-binding data the molecular weights of the glycoprotein monomers were calculated to be 18700 and 17500 for thymus and brain Thy-1 glycoprotein monomers were calculated to be 18700 and 17500 for thymus and brain Thy-1 glycoproteins respectively. The molecular weight of the polypeptide part of the glycoprotein is thus 12500. 3. In the absence of deoxycholate, brain or thymus Thy-1 glycoprotein formed large homogeneous complexes of mol. wt. 270000 or 300000 respectively. The sedimentation coefficient of these was 12.8 S. The complex was only partially dissociated by 4M-guanidinium chloride. 4. After cleavage of brain or thymus Thy-1 glycoprotein with CNBr, two peptides were clearly identified. They were linked by disulphide bonds and both contained carbohydrate. This cleavage suggests there is only one methionine residue per molecule, which is consistent with the above molecular weights and the known amino acid composition.

LIGHT-SCATTERING STUDIES OF SODIUM THYMONUCLEATE

1950 ◽  
Vol 28b (3) ◽  
pp. 96-104 ◽  
Author(s):  
D. B. Smith ◽  
H. Sheffer
Keyword(s):  
Hydrogen Peroxide ◽  
Molecular Weight ◽  
Light Scattering ◽  
Sodium Chloride ◽  
Aqueous Solutions ◽  
Salt Solution ◽  
Molecular Weights ◽  
Three Samples ◽  
Two Samples ◽  
Viscous Solution

The scattering of light by aqueous solutions of three different samples of sodium thymonucleate has been investigated. It was found that one sample in water consisted of randomly coiled molecules of molecular weight greater than 24 × 106. A second sample gave a less viscous solution in water and was only partially coiled, the coiling of the molecules being increased by the addition of a small amount of sodium chloride. In dilute salt solution the molecular weights of all three samples were greater than 3.7 × 106. Two samples of nucleate were degraded in solution by irradiation with ultraviolet light in the presence of hydrogen peroxide. In both cases the nucleate was converted into material consisting of rodlike molecules, 2400 Å in length and having a molecular weight of 750,000.

scholarly journals Haemoglobin from the tadpole shrimp, Lepidurus apus lubbocki Characterization of the molecule and determination of the number of polypeptide chains

1979 ◽  
Vol 183 (2) ◽  
pp. 325-330 ◽  
Author(s):  
E Ilan ◽  
E Daniel
Keyword(s):  
Molecular Weight ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sedimentation Coefficient ◽  
Sedimentation Equilibrium ◽  
Guanidinium Chloride ◽  
Tadpole Shrimp ◽  
Polypeptide Chains

Haemoglobin from the tadpole shrimp, Lepidurus apus lubbocki, was found to have a sedimentation coefficient (s020,w) of 19.3 +/- 0.2 S and a molecular weight, as determined by sedimentation equilibrium, of 798000 +/- 20000. The amino acid composition showed the lack of cysteine and cystine residues. A haem content of 3.55 +/- 0.03% was determined, corresponding to a minimal mol.wt. of 17400 +/- 200. The pH-independence in the range pH 5-11 of the sedimentation coefficient indicates a relatively high stability of the native molecule. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis gave one band with mobility corresponding to a mol.wt. of 34000 +/- 1500. The molecular weight of the polypeptide chain was determined to be 32800 +/- 800 by sedimentation equilibrium in 6 M-guanidinium chloride and 0.1 M-2-mercaptoethanol. The findings indicate that Lepidurus haemoglobin is composed of 24 identical polypeptide chains, carrying two haem groups each.

PURIFICATION AND PROPERTIES OF A PROTEASE FROM PENICILLIUM CYANEO-FULVUM

1960 ◽  
Vol 38 (1) ◽  
pp. 969-980 ◽  
Author(s):  
Kartar Singh ◽  
S. M. Martin
Keyword(s):  
Molecular Weight ◽  
Enzyme Activity ◽  
Proteolytic Enzyme ◽  
Ethylenediaminetetraacetic Acid ◽  
Alkaline Proteases ◽  
Plasma Albumin ◽  
Metal Chelating ◽  
Bovine Plasma ◽  
Purification And Properties ◽  
Optimum Ph

A proteolytic enzyme present in culture filtrates of Penicillium cyaneo-fulvum was purified approximately 100-fold. In the ultracentrifuge the enzyme behaved as a homogeneous protein, but on electrophoresis some contamination was apparent. The molecular weight of the enzyme was estimated to be about 45,000.The protease hydrolyzed casein and denatured haemoglobin, gelatin, and native bovine plasma albumin but not native or denatured ovalbumin. It also coagulated milk. The optimum pH for caseolysis was 9.5 to 11.0. Metal chelating- and sulphydryl-reagents did not affect enzyme activity but zinc and mercurous ions inhibited the enzyme, the inhibition being reversed with ethylenediaminetetraacetic acid (EDTA). Soybean trypsin inhibitor was without effect on the enzyme whereas ovomucoid inhibited the enzyme. Although it is similar in some respects to other alkaline proteases, the P. cyaneo-fulvum enzyme does not appear to be identical with any one of them.

scholarly journals Characterization of the extracellular haemoglobin of Haemopsis sanguisuga (L.)

1976 ◽  
Vol 153 (3) ◽  
pp. 589-596 ◽  
Author(s):  
E J Wood ◽  
L J Mosby ◽  
M S Robinson
Keyword(s):  
Molecular Weight ◽  
Electron Microscope ◽  
Gel Electrophoresis ◽  
Root Nodules ◽  
Sedimentation Coefficient ◽  
Soya Bean ◽  
Sedimentation Equilibrium ◽  
Helical Content ◽  
Polypeptide Chains

The haemoglobin from the blood of the horseleech, Haemopsis sanguisuga (L.), had a sedimentation coefficient, SO20, w, of 59.11 +/- 0.55 S, and a molecular weight as determined by sedimentation equilibrium of 3.71 × 10(6)+/-9904 × 10(6). In the electron microscope the molecule appeared to be made up of two hexagonal plates, as is found with other worm haemoglobins, with dimensions 24.4+/-2.0 nm (across the hexagon) and 15.2+/-1.4 nm (height). The amino acid composition and spectrum were closely similar to those of the haemoglobins of other annelids (e.g. Lumbricus). The α-helical content, calculated from circular-dichroism measurements in the far-u.v. region, was 56-63%. The haem content was 2.49%, corresponding to a minimum molecular weight per haem group of 24 800, but detergent-gel electrophoresis indicated the presence of polypeptide chains of mol.wts. 12 600, 14 800, 15 500 and 25 100. The pH-induced dissociation of the native molecule yielded compotosol of Soya-bean root nodules.

scholarly journals Self-association of dermatan sulphate proteoglycans from bovine sclera

1981 ◽  
Vol 197 (2) ◽  
pp. 483-490 ◽  
Author(s):  
L Cöster ◽  
L A Fransson ◽  
J Sheehan ◽  
I A Nieduszynski ◽  
C F Phelps
Keyword(s):  
Molecular Weight ◽  
Light Scattering ◽  
Guanidine Hydrochloride ◽  
Apparent Molecular Weight ◽  
Sedimentation Equilibrium ◽  
Gel Chromatography ◽  
Side Chains ◽  
Dermatan Sulphate ◽  
Molecular Weights ◽  
High Particle

1. Two proteodermatan sulphate fractions (I and II) from bovine sclera were studied by gel chromatography, light-scattering and ultracentrifugation under various conditions. 2. Gel chromatography of proteoglycans in the absence or presence of hyaluronate was performed under associative conditions. No effect on the elution profile was noted. 3. Ultracentrifugation experiments (sedimentation-velocity and sedimentation-equilibrium) with proteoglycan I and II in 6 M-guanidine hydrochloride gave molecular weights (Mw) of 160000-220000 and 70000-100000 respectively. As the protein contents were 45% and 60% respectively, it may be calculated that proteoglycan I contained four to five side chains, whereas proteoglycan II contained one or two. Sedimentation-equilibrium runs performed in 0.15 M-NaCl gave an apparent molecular weight (Mw) of 500000-800000 for proteoglycan I and 90000-110000 for proteoglycan II. 4. In light-scattering experiments both proteoglycans I and II yielded high particle weights in 0.15 M-NaCl (3.1 × 10(6) and 3.4 × 10(6) daltons respectively). In the presence of 6 M-guanidine hydrochloride the molecular weights decreased to 410000 and 130000 respectively. The particle weights in 0.15 M-NaCl were not altered by the addition of hyaluronate or hyaluronate oligosaccharides. 5. The dermatan sulphate side chains of scleral proteoglycans (L-iduronate/D-glucuronate ratio 7:13) gave a particle weight of 100000 daltons in 0.15 M-NaCl. In 1.00 M-KCl/0.02M-EDTA the molecular weight was 24000. Addition of free scleral dermatan sulphate chains to a solution of proteoglycan II promoted further multimerization of the macromolecule.

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