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.

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.

scholarly journals Anti-neutrophil cytoplasm antibodies in Wegener's granulomatosis recognize an elastinolytic enzyme.

1990 ◽  
Vol 171 (1) ◽  
pp. 357-362 ◽  
Author(s):  
J Lüdemann ◽  
B Utecht ◽  
W L Gross
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Sequence Analysis ◽  
Enzymatic Activity ◽  
Serine Proteinase ◽  
Human Neutrophils ◽  
Target Antigen ◽  
Proteinase 3 ◽  
Serine Proteinases ◽  
Terminal Amino

The target antigen of anti-neutrophil cytoplasm antibodies (ACPA; also known as ANCA) was isolated by affinity chromatography from supernatants of human neutrophils, stimulated with phorbol ester to induce degranulation. Sequence analysis of the antigen revealed 17 NH2-terminal amino acids (IVGGHEAQPHIRPIYMA), which have considerable sequence homology with known serine proteinases. Investigation of the enzymatic activity showed that the antigen is a neutral serine proteinase that is able to cleave elastin. Since the molecular weight of the antigen, its substrate specificity, and its inhibitor profile reported in this study are identical with those reported recently for proteinase 3, we conclude that ACPA are most probably directed against proteinase 3.

scholarly journals Rabbit Tamm–Horsfall urinary glycoprotein. Chemical composition and subunit structure

1971 ◽  
Vol 122 (5) ◽  
pp. 623-631 ◽  
Author(s):  
Anne M. S. Marr ◽  
A. Neuberger ◽  
Wendy A. Ratcliffe
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Chemical Composition ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Cross Reactivity ◽  
Subunit Structure ◽  
Terminal Amino

1. Tamm–Horsfall glycoprotein from rabbit urine has been isolated and characterized. The homogeneity of the preparation has been established by a variety of procedures including disc gel electrophoresis and ultracentrifugation in aqueous solution, sodium dodecyl sulphate and formic acid. 2. The chemical composition has been determined and a carbohydrate content of approx. 31% was obtained. The relative contents of the amino acids were shown to be very similar to those in human Tamm–Horsfall glycoprotein. A trace of lipid was also detected. 3. Leucine was identified as the only N-terminal amino acid. 4. The subunit structure was investigated in the presence of sodium dodecyl sulphate by gel filtration and disc gel electrophoresis. These studies indicated that the subunit possessed a molecular weight of approx. 84000±6000. A similar value was obtained after reduction and S-alkylation of the glycoprotein indicating that the disulphide bonds were all intrachain. 5. A minimum value for the chemical molecular weight of 85000±6000 was obtained from the number of N-terminal amino acids released by cyanogen bromide cleavage of the glycoprotein. 6. The immunological properties of the glycoprotein were studied. Cross reactivity was demonstrated between human Tamm–Horsfall glycoprotein and a guinea-pig anti-rabbit Tamm–Horsfall antiserum.

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.

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 Chemical and physical characterization of a proline-rich polypeptide from sheep colostrum

1981 ◽  
Vol 199 (1) ◽  
pp. 9-15 ◽  
Author(s):  
M Janusz ◽  
K Starościk ◽  
M Zimecki ◽  
Z Wieczorek ◽  
J Lisowski
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Room Temperature ◽  
Proteolytic Enzymes ◽  
Gel Filtration ◽  
Guanidinium Chloride ◽  
Terminal Amino Acid ◽  
Polyproline Ii ◽  
Terminal Amino

A proline-rich polypeptide isolated from sheep colostrum is described. The molecular weight of the polypeptide determined by gel filtration is 17 200. However, in the presence of guanidinium chloride the molecular weight found is about 6000. The polypeptide contains about 22% of proline, a high proportion of non-polar amino acids, a low percentage of glycine, and no alanine, arginine and cysteine residues. The only N-terminal amino acid found is leucine. C.d. spectra in water and in 50% (v/v) trifluoroethanol suggest the presence of block sequences of proline residues forming helices of polyproline II type. The proline-rich polypeptide is soluble at 4 degrees C but is reversibly precipitated on warming to room temperature. Maximal precipitation is observed at pH 4.6 and at ionic strength above 0.6. The precipitation depends on the concentration of the polypeptide. No effect of other proteins, Ca2+ and Zn2+ ions on the precipitation of the polypeptide was found. The proline-rich polypeptide is not an amphipathic protein. The lack of effect of the polypeptide on proteolytic enzymes ruled out the possibility that it is an inhibitor of proteinases.

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.

THE TERMINAL AMINO ACIDS OF WHEAT GLIADIN

1955 ◽  
Vol 33 (10) ◽  
pp. 1463-1466 ◽  
Author(s):  
L. K. Ramachandran ◽  
W. B. McConnell
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Hydrochloric Acid ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Qualitative Evidence ◽  
Wheat Gliadin ◽  
Terminal Amino

Wheat gliadin has been found by two different methods to contain three N-terminal histidine residues for each molecular weight of 27,000. Trace amounts of N-terminal aspartic acid, glutamic acid, alanine, valine, and serine were also detected in the preparation used. Hydrolysis in boiling hydrochloric acid partially destroyed the di-2,4-dinitrophenyl derivative of histidine. Losses of from 5% to 25% occurred depending upon the time and conditions of hydrolysis. Carboxypeptidase did not release free amino acids from wheat gliadin but qualitative evidence for the occurrence of C-terminal glutamic acid and C-terminal "leucine" was obtained.

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