Disease relevance of AIDS-132114

• In addition, the capacity of E. coli to promote PMN degranulation is dependent on its phenotypic fimbrial expression, a surface characteristic which correlates significantly with its relative surface hydrophobicity as measured by binding to octyl Sepharose [1].
• Sensitization of smooth Salmonella typhimurium 395 MS bacteria with hyper-immune anti-MS immunoglobulin G (IgG) antibodies increased the liability to hydrophobic interaction as assessed by the affinity for a column of Octyl-Sepharose [2].
• One strain, which was identified as Pseudomonas fluorescens GK13 (biovar V), was selected and the extracellular P(3HO) depolymerase of this strain was purified from the culture medium of P(3HO)-grown cells by chromatography with Octyl-Sepharose CL4B and by gel filtration with Superose 12 [3].
• We have purified a unique enzyme, alpha-amino-epsilon-caprolactam racemase 945-fold from an extract of Achromobacter obae by Octyl-Sepharose CL-4B and Thiopropyl-Sepharose 6B and some other chromatographies [4].
• We have identified this molecule in human erythroleukemia and CHRF 288-11 cells by the presence of characteristic core proteins between 92-120 kDa, by its ability to adhere to Octyl Sepharose and by detection of mRNA [5].

High impact information on AIDS-132114

• The HSPG is anchored to the cell surface through phosphatidylinositol (PI) linkages, as evidenced in part by the ability of PI-specific phospholipase C to eliminate binding of the detergent-extracted HSPG to Octyl Sepharose [6].
• The active heparan sulfate proteoglycan can be partially purified by affinity chromatography on thrombospondin-agarose or hydrophobic interaction with octyl-Sepharose [7].
• The purification procedure included ammonium sulfate precipitation and sequential column chromatography on octyl-Sepharose, ATP-agarose, Mono Q fast protein liquid chromatography (FPLC), and hydroxyapatite FPLC [8].
• Two antigenically and structurally related heparan sulfate proteoglycans (HSPG), with masses of 200 and 350 kDa, have been isolated and characterized from bovine renal tubular basement membranes (BTBM) using DEAE-Sephacel, octyl-Sepharose CL-4B, and Propac PA-1 chromatography [9].
• Both CS-PG and HS-PG displayed affinity for octyl sepharose and both were identified in isolated plasma membranes [10].

Chemical compound and disease context of AIDS-132114

• By hydrophobic interaction chromatography on octyl-Sepharose, lipopolysaccharide (LPS) of Escherichia coli Re mutant and of wild-type smooth-form (S-form) Salmonella typhimurium and Salmonella abortus equi is fractionated according to increasing amount of fatty acids [11].
• The squalene-hopene cyclase of the hopanoid- and tetrahymanol-producing Rhodopseudomonas palustris was released from the isolated membranes by CHAPS and purified to homogeneity by successive chromatography on DEAE Sephacel, Octyl Sepharose, and Blue Sepharose [12].

Biological context of AIDS-132114

• One-step calcium-dependent octyl-Sepharose chromatography was used to obtain the two highly purified forms of rPLD alpha, as attested by gel electrophoresis, N-terminal amino acid sequence and mass spectrometry [13].
• The glycoconjugate can be purified by hydrophobic interaction chromatography on octyl-Sepharose; enzymatic hydrolysis with phosphatidylinositol-specific phospholipase C alters the hydrophobic properties of the molecule [14].
• The retention of trypsin, chymotrypsin and their diisopropylphosphoryl derivatives on a support with flexible hydrophobic ligands bonded to the matrix through a spacer (octyl-Sepharose) was correlated with the retention on a support with hydrophobic binding sites incorporated into the rigid matrix of the resin (Spheron) [15].
• The solubilized [3H]mepyramine binding protein was purified 30-fold by Sepharose CL-4B gel filtration, Bio Gel HTP hydroxylapatite, Octyl Sepharose 4B and hydroxylapatite HPLC column chromatographies [16].
• A number of apolar and polar PIM intermediates were labelled when this system was continuously labelled or pulse-chase-labelled with GDP-[3H]Man, and the glycan head groups and the acylation states of these species were determined by chemical and enzymic treatments and octyl-Sepharose chromatography respectively [17].

Anatomical context of AIDS-132114

• This HSPG is an integral plasma membrane component by virtue of its binding to Octyl Sepharose affinity columns and that anti-HSPG antibody staining exhibited a cell surface localization [6].
• Cytochrome P-45011beta has been solubilized and partially purified from bovine adrenal cortex mitochondria by means of chromatography on Octyl-Sepharose CL-4B or DEAE-Sepharose CL-6B [18].
• Characterization of the dermatan sulfate proteoglycans, DS-PGI and DS-PGII, from bovine articular cartilage and skin isolated by octyl-sepharose chromatography [19].
• A ribonuclease P-like activity was partially purified from HeLa cell mitochondria by DEAE-cellulose and octyl-Sepharose chromatography [20].
• Multiple classes of heparan sulfate proteoglycans from fibroblast substratum adhesion sites. Affinity fractionation on columns of platelet factor 4, plasma fibronectin, and octyl-sepharose [21].

Associations of AIDS-132114 with other chemical compounds

• However, as shown by hydrophobic interaction chromatography on phenyl- and octyl-Sepharose 4B, IF proteins and their proteolytic derivatives also appear to have high affinities for aromatic and aliphatic substructures of biologically important molecules [22].
• One type had an Mr of 5-8 X 10(5) as estimated by gel chromatography on Sepharose CL-4B in the presence of 0.1% sodium dodecyl sulfate and lacked hydrophobic properties in that it showed no affinity for octyl-Sepharose and could not be inserted into liposomes [23].
• The detergent-solubilized HSPG bound to octyl-Sepharose columns, whereas the hydrophilic form did not; this latter form, however, was released from the membrane by heparin [24].
• A diacylglycerol (DG) lipase has been purified from a soluble subcellular fraction of bovine aorta by (NH4)2SO4 precipitation in the presence of 5.0% (w/v) Triton X-100, followed by chromatography on DEAE-Sephacel, heparin-Sepharose and octyl-Sepharose in the presence of either CHAPS or Triton X-100 detergents [25].
• The larger one contained the heparan sulphate chains and glycoprotein-type oligosaccharides, whereas the smaller one contained interchain disulphide bond(s) and had affinity for transferrin as well as for octyl-Sepharose [26].

Gene context of AIDS-132114

• The results show that mouse plasma G1 AChE possesses hydrophobic regions, which prevent its binding to the affinity matrix, and afford its interaction with octyl-Sepharose [27].
• The ligand, 3-phosphoglycerate, significantly decreased the amount of phosphoglycerate kinase able to bind to octyl-Sepharose [28].
• The proteoglycans were isolated using either (a) molecular sieve chromatography under conditions where DS-PGI selectively self-associates or (b) chromatography on octyl-Sepharose, which separates DS-PGI from DS-PGII based on differences in the hydrophobic properties of their core proteins [19].
• We purified an 80-kDa Ca2+-independent phospholipase A2 (iPLA2) from rat brain using octyl-Sepharose, ATP-agarose, and calmodulin-agarose column chromatography steps [29].
• Hydrophobic interaction chromatography (HIC) using phenyl- or octyl-Sepharose was used to purify the high density lipoprotein (HDL)-associated acute phase reactant serum amyloid A (SAA) [30].

Analytical, diagnostic and therapeutic context of AIDS-132114

• The calcium- and phospholipid-dependent kinase activity (protein kinase C) was isolated from bovine brains by a combination of DEAE-cellulose chromatography, gel filtration and hydrophobic chromatography on octyl-Sepharose and phenyl-Sepharose [31].
• By using octyl-Sepharose chromatography to isolate holocytochrome c oxidase and by extracting the holoenzyme with aprotic organic solvents and fractionating these extracts by reversed phase high performance liquid chromatography, it is possible to isolate several milligrams of each of these subunits [32].
• Molecular sieve high performance liquid chromatography HPLC, reverse phase HPLC on an octylsilyl (C8) column, and hydrophobic chromatography on octyl-Sepharose CL-4B all confirm a similar degree (i.e. greater than 90%) of homogeneity [33].
• The GIPLs were the only glycolipids detected and were purified by octyl-Sepharose and thin layer chromatographies [34].
• Cells were disrupted by ultrasonic treatment and the enzyme was purified from the cell-free extract by three successive liquid column chromatographies (Sepharose CL4B/octyl-Sepharose CL4B, DE52 DEAE-cellulose and concanavalin A-Sepharose 4B) [35].

References