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 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.

Polyethyleneimine-assisted synthesis of high-quality platinum/graphene hybrids: the effect of molecular weight on electrochemical properties

2015 ◽  
Vol 3 (22) ◽  
pp. 12000-12004 ◽  
Author(s):  
Xueqing Gao ◽  
Yumei Li ◽  
Qi Zhang ◽  
Shuni Li ◽  
Yu Chen ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Formic Acid ◽  
Electrochemical Properties ◽  
Electrocatalytic Activity ◽  
Oxidation Reaction ◽  
Formic Acid Oxidation ◽  
Acid Oxidation ◽  
High Quality ◽  
Formic Acid Oxidation Reaction

The molecular weight of PEI remarkably affected the electrocatalytic activity of Pt/RGO hybrids for the formic acid oxidation reaction.

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.

The subunit and polypeptide structure of hexosaminidases from human placenta

1980 ◽  
Vol 58 (4) ◽  
pp. 287-294 ◽  
Author(s):  
D. Mahuran ◽  
J. A. Lowden
Keyword(s):  
Molecular Weight ◽  
Disulfide Bond ◽  
Hydrophobic Interaction ◽  
Sodium Dodecyl ◽  
Performic Acid ◽  
Acid Oxidation ◽  
Α Subunit ◽  
Chain Dimer ◽  
Α Chain ◽  
Polypeptide Structure

Previous reports have indicated that the hexosaminidases (HEX) are tetrameric enzymes composed of either two dimers of β chains (HEX B) or a β-chain dimer and an α-chain dimer (HEX A). HEX S contains only α chains. The apparent molecular weight of both α and β chains is 25 000. We isolated and purified HEX A and B more than 6000-fold. From HEX A we prepared HEX B and a more anodically migrating HEX S, which contained only α chains. After either extensive reduction and alkylation or performic acid oxidation, HEX B gave only a single protein band in polyacrylamide gel electrophoresis in sodium dodecyl sulfate; HEX A consistently gave two bands indicating it contained chains of two different molecular weights. Other reports note two bands in HEX A but have dismissed the high molecular weight band as a dimer caused by either hydrophobic interaction or an unbroken disulfide bond. To rule out hydrophobic interaction, we determined molecular weight by gel filtration in 6 M guanidine–HC1. To ensure complete disulfide bond breakage we used a harsher reduction and alkylation procedure than previously employed by others. The results were then confirmed by the use of two performic acid oxidation techniques, the stronger method resulting in extensive peptide bond oxidation. Samples of HEX A under reduction and alkylation or the weaker performic acid oxidation procedure, again chromatographed as two approximately equal peaks (50 000 and 25 000). HEX B, and the HEX B prepared from HEX A, resulted in one 25 000-dalton peak. HEX S chromatographed as a single 50 000 peak. We conclude that either the α chain in HEX has a molecular weight of 50 000 with one α chain per α subunit or that two 25 000-dalton chains are united by a nondisulfide crosslink (e.g., an isopeptide bond).

DEGRADATION BY HYDRAZINE OF BOVINE PLASMA ALBUMIN AND LYSOZYME

1960 ◽  
Vol 38 (1) ◽  
pp. 715-726 ◽  
Author(s):  
Madeleine Champagne ◽  
David B. Smith
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Hydrazine Hydrate ◽  
Plasma Albumin ◽  
Bovine Plasma ◽  
Terminal Amino

The effect of hydrazine and hydrazine hydrate on bovine plasma albumin and lysozyme at 5° and 20 °C has been studied by viscosity, sedimentation, and molecular weight measurements. The appearance of new N-terminal amino acids and peptides has been demonstrated. The effect of these reagents is an initial unfolding of the molecule followed by slow, non-random fission to smaller particles.

PURIFICATION AND PROPERTIES OF A PROTEASE FROM PENICILLIUM CYANEO-FULVUM

1960 ◽  
Vol 38 (9) ◽  
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.

DEGRADATION BY HYDRAZINE OF BOVINE PLASMA ALBUMIN AND LYSOZYME

1960 ◽  
Vol 38 (7) ◽  
pp. 715-726 ◽  
Author(s):  
Madeleine Champagne ◽  
David B. Smith
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Hydrazine Hydrate ◽  
Plasma Albumin ◽  
Bovine Plasma ◽  
Terminal Amino

The effect of hydrazine and hydrazine hydrate on bovine plasma albumin and lysozyme at 5° and 20 °C has been studied by viscosity, sedimentation, and molecular weight measurements. The appearance of new N-terminal amino acids and peptides has been demonstrated. The effect of these reagents is an initial unfolding of the molecule followed by slow, non-random fission to smaller particles.

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