Biomaterial Database

Isolation and partial characterization of a plasma membrane-enriched fraction of Blastomyces dermatitidis. 1990

V P Chaturvedi, and S Chaturvedi, and H S Randhawa, and Z U Khan, and B K Puri

National Reference Centre for Respiratory Mycoses (ICMR), University of Delhi, India.

The isolation and characterization of a plasma membrane-enriched fraction is reported from the pathogenic fungus Blastomyces dermatitidis employing a simplified and inexpensive procedure. The yeast cells, suspended in an osmotic stabilizer buffer, were subjected to gentle mechanical disruption followed by a three-step differential centrifugation to obtain a 40,000 x g sediment. This fraction showed 2.7- and 3.3-fold relative enrichment of the plasma membrane marker enzymes Mg2(+)-ATPase and 5'-nucleotidase, respectively, with modest cross-contamination of other intracellular membranes. The fraction comprised approximately 49% protein, 31% carbohydrate, 11% phospholipids and 9% sterol with sterol to phospholipid molar ratio of 1.1. Transmission electron microscopy of the plasma membrane-enriched fraction showed homogeneous vesicles with a tripartite unit membrane of 115 A thickness.

UI	MeSH Term	Description	Entries
D008563	Membrane Lipids	Lipids, predominantly phospholipids, cholesterol and small amounts of glycolipids found in membranes including cellular and intracellular membranes. These lipids may be arranged in bilayers in the membranes with integral proteins between the layers and peripheral proteins attached to the outside. Membrane lipids are required for active transport, several enzymatic activities and membrane formation.	Cell Membrane Lipid,Cell Membrane Lipids,Membrane Lipid,Lipid, Cell Membrane,Lipid, Membrane,Lipids, Cell Membrane,Lipids, Membrane,Membrane Lipid, Cell,Membrane Lipids, Cell
D008565	Membrane Proteins	Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.	Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D008854	Microscopy, Electron	Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.	Electron Microscopy
D010743	Phospholipids	Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.	Phosphatides,Phospholipid
D001758	Blastomyces	A genus of onygenacetous mitosporic fungi whose perfect state is Ajellomyces (see ONYGENALES). The species Blastomyces dermatitidis (perfect state is Ajellomyces dermatitidis) causes blastomycosis.	Ajellomyces dermatitidis,Blastomycoides dermatitidis,Blastomyces dermatitidis
D002241	Carbohydrates	A class of organic compounds composed of carbon, hydrogen, and oxygen in a ratio of Cn(H2O)n. The largest class of organic compounds, including STARCH; GLYCOGEN; CELLULOSE; POLYSACCHARIDES; and simple MONOSACCHARIDES.	Carbohydrate
D002458	Cell Fractionation	Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.	Cell Fractionations,Fractionation, Cell,Fractionations, Cell
D002462	Cell Membrane	The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.	Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D015720	5'-Nucleotidase	A glycoprotein enzyme present in various organs and in many cells. The enzyme catalyzes the hydrolysis of a 5'-ribonucleotide to a ribonucleoside and orthophosphate in the presence of water. It is cation-dependent and exists in a membrane-bound and soluble form. EC 3.1.3.5.	5'-AMP Nucleotidase,AMP Phosphatase,Adenylate Phosphatase,Antigens, CD73,CD73 Antigens,Cytidylate Phosphatase,Ecto-5'-Nucleotidase,IMP Nucleotidase,IMP Phosphatase,Inosinate Phosphatase,Pyrimidine 5'-Nucleotidase,Thymidine Phosphatase,Uridylate 5'-Nucleotidase,5'-Nucleotidase Phosphoribolase,Antigen, CD73,IMPase,5' AMP Nucleotidase,5' Nucleotidase,5' Nucleotidase Phosphoribolase,CD73 Antigen,Ecto 5' Nucleotidase,Pyrimidine 5' Nucleotidase,Uridylate 5' Nucleotidase
D017301	Ca(2+) Mg(2+)-ATPase	An enzyme that catalyzes the hydrolysis of ATP and is activated by millimolar concentrations of either Ca(2+) or Mg(2+). Unlike CA(2+)-TRANSPORTING ATPASE it does not require the second divalent cation for its activity, and is not sensitive to orthovanadate. (Prog Biophys Mol Biol 1988;52(1):1). A subgroup of EC 3.6.1.3.	ATPase, Calcium Magnesium,ATPase, Magnesium,Adenosinetriphosphatase, Calcium, Magnesium,Adenosinetriphosphatase, Magnesium,Calcium Magnesium ATPase,Calcium Magnesium Adenosinetriphosphatase,Magnesium ATPase,Magnesium Adenosinetriphosphatase,Adenosine Triphosphatase, Calcium, Magnesium,Adenosine Triphosphatase, Magnesium,Ca Mg-ATPase,Ca2+-Mg2+ ATPase,Calcium Magnesium Adenosine Triphosphatase,Mg2+-ATPase,Mg2+-Dependent ATPase,ATPase, Ca2+-Mg2+,ATPase, Mg2+-Dependent,Adenosinetriphosphatase, Calcium Magnesium,Ca Mg ATPase,Ca2+ Mg2+ ATPase,Magnesium Adenosine Triphosphatase,Mg2+ ATPase,Mg2+ Dependent ATPase