scholarly journals Molecular Weight and N-Terminal Amino Acids of the Proteins of the Phosvitin Fraction of Avian Egg Yolk

1976 ◽  
Vol 55 (2) ◽  
pp. 790-795 ◽  
Author(s):  
R.C. Shantz ◽  
L.E. Dawson
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Egg Yolk ◽  
Terminal Amino ◽  
Avian Egg

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.

N-TERMINAL AMINO ACIDS OF THE PROTEINS OF THE FLOATING FRACTION OF EGG YOLK

1958 ◽  
Vol 36 (9) ◽  
pp. 951-952 ◽  
Author(s):  
David B. Smith ◽  
K. J. Turner
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Primary Structure ◽  
Egg Yolk ◽  
Minor Components ◽  
Terminal Amino Acid ◽  
Hen’S Egg ◽  
Terminal Amino

Lysine is the major N-terminal amino acid of both the soluble and insoluble fractions of the floating lipoprotein of hen's egg yolk, which suggests a common primary structure. Several minor components are also present in both fractions.

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.

N-TERMINAL AMINO ACIDS OF THE PROTEINS OF THE FLOATING FRACTION OF EGG YOLK

1958 ◽  
Vol 36 (1) ◽  
pp. 951-952 ◽  
Author(s):  
David B. Smith ◽  
K. J. Turner
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Primary Structure ◽  
Egg Yolk ◽  
Minor Components ◽  
Terminal Amino Acid ◽  
Hen’S Egg ◽  
Terminal Amino

Lysine is the major N-terminal amino acid of both the soluble and insoluble fractions of the floating lipoprotein of hen's egg yolk, which suggests a common primary structure. Several minor components are also present in both fractions.

TERMINAL AMINO ACIDS OF EGG YOLK LIPOPROTEINS

1961 ◽  
Vol 39 (6) ◽  
pp. 1075-1084 ◽  
Author(s):  
J. M. Neelin ◽  
W. H. Cook
Keyword(s):  
Amino Acids ◽  
Average Molecular Weight ◽  
Egg Yolk ◽  
Water Soluble ◽  
Terminal Amino Acid ◽  
Physical Measurements ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Protein Moiety ◽  
Egg Yolk Lipoproteins

The N-terminal amino acids of the two lipovitellins and lipovitellenin of egg yolk have been determined. α-Lipovitellin and β-lipovitellin were separated by chromatography on hydroxyapatite but the lipovitellenin in the low-density fraction did not yield stable and reproducible chromatographic components. The major N-terminal amino acids recovered as dinitrophenyl derivatives from all three fractions were arginine and lysine. Further purification removed several minor components, but tyrosine and serine remained in vitellin, and alanine and serine in vitellenin. The principal C-terminal amino acid of vitellenin was glutamic acid. Arginine appeared to be the chief N-terminal residue but difficulty in purifying the water-soluble dinitrophenyl-amino acids led to highly variable yields; thus the total calculated amounts of terminal amino acids ranged from 9 to 35 micromoles per gram of protein. At least two polypeptide chains are indicated, with an average molecular weight less than the size of the total protein moiety of the parent lipoprotein. This is consistent with reported physical measurements in formic acid. The three lipoprotein fractions are indistinguishable on the basis of their terminal amino acids.

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.

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.

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.

CHARACTERIZATION OF THE PIGMENT OF MICROCOCCUS VIOLAGABRIELLAE

1964 ◽  
Vol 10 (5) ◽  
pp. 659-675 ◽  
Author(s):  
J. N. Campbell ◽  
J. L. Nichols ◽  
Sheila A. Berry
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Cross Reactivity ◽  
Low Molecular Weight ◽  
Terminal Amino Acid ◽  
Iron Chelate ◽  
Peptide Moiety ◽  
Terminal Amino

Production of the red insoluble pigment by Micrococcus violagabriellae was studied. Pigmentation was found to require oxygen and high levels of iron and to be stimulated by tryptophan alone among the amino acids. The pigment was isolated, purified, and analyzed chemically and spectrophotometrically. It was found to be similar to pulcherrimin from Candida pulcherrima. Immunological cross reactivity and analysis of derivatives confirmed the similarity between the bacterial and yeast pigments. From these data it is postulated that the pigment is an iron chelate of pulcherriminic acid with an associated low molecular weight peptide moiety with glycine as the sole N-terminal amino acid. The pigment appears to differ from that of C. pulcherrima solely with respect to this peptide and in the mode of aggregation of the molecule.

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