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European Journal of Biochemistry Jan 1969
Topics: Brucella; Brucella abortus; Chemical Phenomena; Chemistry; Chromatography, Gas; Chromatography, Thin Layer; Cyclopropanes; Fatty Acids; Infrared Rays; Lipids; Palmitic Acids; Species Specificity; Spectrophotometry; Spectrum Analysis
PubMed: 4978225
DOI: 10.1111/j.1432-1033.1969.tb19621.x -
European Journal of Biochemistry Jun 1977Two glycosphingolipids, the carbohydrate portion of which consisted of galactose, glucose and N-acetylgalactosamine, have been isolated from the aqueous phase of...
Two glycosphingolipids, the carbohydrate portion of which consisted of galactose, glucose and N-acetylgalactosamine, have been isolated from the aqueous phase of buffered tetrahydrofuran extract of dog gastric mucosa. The structures of these glycolipids were identified by partial acid hydrolysis, sequential degradation with specific glycosidases and methylation analysis. The structure of glycolipid I (GalNAcalpha1 leads to 3GalNAcbeta1 leads to 3Galalpha1 leads to 4Galbeta1 leads to 4Glc leads to ceramide) was found to be identical to that of Forssman hapten. The branched structure of glycolipid II, as determined by the combination of enzymatic degradation and comparison of the permethylation products of the enzyme-degraded compounds, is proposed to be: See Source.
Topics: Acetylgalactosamine; Animals; Ceramides; Chromatography, Gas; Dogs; Fatty Acids; Forssman Antigen; Galactose; Gastric Mucosa; Glucose; Glycolipids; Glycosphingolipids; Molecular Conformation; Oligosaccharides; Solubility
PubMed: 891524
DOI: 10.1111/j.1432-1033.1977.tb11619.x -
European Journal of Biochemistry Aug 1969
Topics: Adenoviridae; Amino Acids; Animals; Antigens; Carbohydrates; Carcinoma; Cell Line; Chromatography, Gel; Electrophoresis; Humans; Immune Sera; Immunoelectrophoresis; Methods; Microscopy, Electron; Mouth Neoplasms; Quaternary Ammonium Compounds; Rabbits; Solubility; Ultracentrifugation; Viral Proteins; Virus Cultivation
PubMed: 5388113
DOI: 10.1111/j.1432-1033.1969.tb00663.x -
Journal of Biochemistry Nov 1970
Topics: Amino Acids; Animals; Dolphins; Electrophoresis; Ferritins; Fishes; Horses; Iron; Isoelectric Focusing; Microscopy, Electron; Phosphates; Spectrophotometry; Spleen; Ultracentrifugation
PubMed: 5530156
DOI: 10.1093/oxfordjournals.jbchem.a129401 -
The Journal of Biological Chemistry Oct 1978
Topics: Animals; Carbohydrates; Heparin; Intestinal Mucosa; Models, Molecular; Molecular Conformation; Molecular Weight; Proteoglycans; Rats; Skin; Swine
PubMed: 690122
DOI: No ID Found -
The Biochemical Journal Mar 1975The isolation of a highly purified phosphoprotein, previously named protein A, from human parotid saliva is described. This protein has an unusually high amount of...
The isolation of a highly purified phosphoprotein, previously named protein A, from human parotid saliva is described. This protein has an unusually high amount of glycine, proline and dicarboxylic amino acids. Together these amino acids account for 80% of all residues. The protein contains 1.9mol of P/mol of protein, probably as phosphate in an ester linkage to serine, and about 0.5% carbohydrate, but no hexosamine. The N-terminal is blocked and the following C-terminal sequence is proposed: -Aal-Asp-Ser-Gln-Gly-Arg-Arg. The sioelectric point is 4.43. The molecular weight of the protein determined by ultracentrifugation is 9900 and from chemical analyses 11000. Circular-dichrosim and nuclea-magnetic-resonance spectra indicate the absence of polyproline and triple-helical-collagen-like structure for the protein. There is little restriction on the orientation of the single phenylalanine residue in the protein., but there is also an indication of conformational restraint in the protein.
Topics: Amino Acids, Dicarboxylic; Carbohydrates; Glycine; Hexosamines; Humans; Isoelectric Focusing; Magnetic Resonance Spectroscopy; Models, Structural; Molecular Weight; Parotid Gland; Peptide Chain Termination, Translational; Phosphates; Phosphoproteins; Proline; Protein Conformation; Saliva; Serine
PubMed: 1156372
DOI: 10.1042/bj1450557 -
The Biochemical Journal Oct 19681. A glycoprotein extracted by cold alkali from the walls of human aorta was purified by chromatography on DEAE-cellulose. 2. The compound was electrophoretically...
1. A glycoprotein extracted by cold alkali from the walls of human aorta was purified by chromatography on DEAE-cellulose. 2. The compound was electrophoretically homogeneous and essentially so by chromatography on DEAE-cellulose. Ultracentrifugal examination revealed two components, and it is suggested that the faster-sedimenting component represents an aggregated form of the glycoprotein. 3. Glycoprotein preparations contained approx. 8% of carbohydrate. Digestion with Pronase yielded a glycopeptide fraction containing all the carbohydrate of the glycoprotein. The glycopeptide, of molecular weight about 7800, contained sialic acid, galactose, mannose, fucose and hexosamine in the approximate molar proportions 5:10:5:2:11. Sialic acid was terminal with respect to the polysaccharide chains. 4. Both elastase and elastomucoproteinases exhibited proteolytic activity towards the glycoprotein. Studies by other investigators have led to the conclusion that elastomucoproteinases attack protein-carbohydrate complexes occurring in intimate association with elastin in aorta and other tissues, and it is suggested that the glycoprotein may be identified with one of these compounds.
Topics: Adolescent; Adult; Age Factors; Aged; Aorta, Thoracic; Carbohydrates; Cellulose; Centrifugation; Child; Child, Preschool; Chromatography, Ion Exchange; Elastin; Electrophoresis; Endopeptidases; Fucose; Galactose; Glycoproteins; Hexosamines; Humans; Infant; Infant, Newborn; Mannose; Middle Aged; Molecular Weight; Neuraminic Acids; Pancreatic Elastase; Polysaccharides
PubMed: 5696869
DOI: 10.1042/bj1090883 -
The Journal of Biological Chemistry Nov 1977The polypeptide and lipid components of the crystallinelipoprotein-phosphoprotein from the yolk system of Xenopus laevis are described. This lipoprotein complex contains...
The polypeptide and lipid components of the crystallinelipoprotein-phosphoprotein from the yolk system of Xenopus laevis are described. This lipoprotein complex contains 17% lipid of which 75% is phospholipid. The phospholipid fraction consists of mostly phosphatidylcholine and phosphatidylethanolamine. The neutral lipid fraction contains mainly triglyceride. The phosphoprotein, phosvitin, has been separated from the lipoprotein, lipovitellin, by classical methods. Three polypeptide chains can be observed in the lipoprotein and their molecular weights as determined by sodium dodecyl sulfate gel electrophoresis are 105,500, 35,500, and 32,000. Phosvitin behaves abnormally on these gels, but analysis of the results suggests Mr = approximately 16,000 to 19,000/polypeptide chain. The lipovitellin component of the yolk complex contains approximately 100 bound lipid molecules/dimer. The stoichiometry of the components of this crystalline lipoprotein system is discussed in terms of the results obtained in this study and those of other workers.
Topics: Amino Acids; Animals; Egg Yolk; Electrophoresis, Polyacrylamide Gel; Female; Lipoproteins; Molecular Weight; Phosphatidylcholines; Phosphatidylethanolamines; Phosphoproteins; Phosvitin; Xenopus
PubMed: 914850
DOI: No ID Found -
The Journal of Biological Chemistry Sep 1971
Topics: Animals; Cholesterol; Chromatography, Gas; Chromatography, Thin Layer; Esters; Ethers; Fatty Acids; Fatty Acids, Nonesterified; Hydrogen-Ion Concentration; Lipids; Male; Methylation; Mitochondria, Muscle; Phosphatidylcholines; Phosphatidylethanolamines; Phospholipids; Rats; Sarcolemma; Sarcoplasmic Reticulum; Sphingomyelins; Triglycerides
PubMed: 5096085
DOI: No ID Found -
Journal of Bacteriology May 1984Electron microscopy and microprobe X-ray analysis were used to study metachromatic inclusions of Spirillum itersonii , Corynebacterium diphtheriae, and Micrococcus...
Electron microscopy and microprobe X-ray analysis were used to study metachromatic inclusions of Spirillum itersonii , Corynebacterium diphtheriae, and Micrococcus luteus. In situ metachromatic inclusions were electron dense and contained phosphorus and divalent cations. Metachromatic inclusions isolated by anion-exchange column chromatography and by isoosmolar Metrizamide density gradient centrifugation were similar in composition to in situ inclusions.
Topics: Calcium; Centrifugation, Density Gradient; Chromatography, Ion Exchange; Chromogenic Compounds; Corynebacterium diphtheriae; Cytoplasmic Granules; Electron Probe Microanalysis; Magnesium; Micrococcus; Phosphorus; Potassium; Proteins; Spirillum
PubMed: 6427179
DOI: 10.1128/jb.158.2.441-446.1984