λ High-salt Buffer

2006 ◽  
Vol 2006 (1) ◽  
pp. pdb.rec298
Keyword(s):  
High Salt ◽  
High Salt Buffer

Improved DEAE-Sephadex column chromatography in measuring amylase in serous ovarian neoplasms, and results for 13 cases.

1982 ◽  
Vol 28 (10) ◽  
pp. 2095-2098 ◽  
Author(s):  
J J Zakowski ◽  
D E Bruns
Keyword(s):  
Ovarian Tumors ◽  
High Salt ◽  
Chromatographic Behavior ◽  
Sephadex Column ◽  
Tumor Tissues ◽  
Constant Feature ◽  
High Salt Buffer ◽  
Acidic Nature ◽  
Serous Ovarian Neoplasms ◽  
Cyst Fluids

Abstract We describe a column-chromatographic method for measuring amylase activity in cyst fluids of serous ovarian tumors. Using this technique, we confirm and extend the previous report of an "acidic" amylase in serous ovarian tumor cyst fluids. This form of the enzyme was eluted from DEAE-Sephadex mini-columns with a high-salt buffer. It accounted for 45 to 100% of the amylase in 13 cyst fluids. This "high-salt" amylase was also present in the tumor tissues. The acidic nature of the amylase does not appear to be due to sialic acid residues, because the chromatographic behavior of the amylase is unaffected by treatment with neuraminidase. We conclude that the "acidic" amylase reported previously in two serous ovarian tumors is a constant feature of these tumors and that it is distinct from the sialylated tumor amylase described by others.

scholarly journals Affinity Purification of DNA and RNA from Environmental Samples with Peptide Nucleic Acid Clamps

2000 ◽  
Vol 66 (8) ◽  
pp. 3438-3445 ◽  
Author(s):  
Darrell P. Chandler ◽  
Jennie R. Stults ◽  
Sharon Cebula ◽  
Beatrice L. Schuck ◽  
Derek W. Weaver ◽  
...  
Keyword(s):  
Nucleic Acid ◽  
Environmental Samples ◽  
Affinity Purification ◽  
High Salt ◽  
Disodium Edta ◽  
Dna And Rna ◽  
Target Dna ◽  
Low Salt ◽  
Absolute Detection Limit ◽  
High Salt Buffer

ABSTRACT Bispeptide nucleic acids (bis-PNAs; PNA clamps), PNA oligomers, and DNA oligonucleotides were evaluated as affinity purification reagents for subfemtomolar 16S ribosomal DNA (rDNA) and rRNA targets in soil, sediment, and industrial air filter nucleic acid extracts. Under low-salt hybridization conditions (10 mM NaPO4, 5 mM disodium EDTA, and 0.025% sodium dodecyl sulfate [SDS]) a PNA clamp recovered significantly more target DNA than either PNA or DNA oligomers. The efficacy of PNA clamps and oligomers was generally enhanced in the presence of excess nontarget DNA and in a low-salt extraction-hybridization buffer. Under high-salt conditions (200 mM NaPO4, 100 mM disodium EDTA, and 0.5% SDS), however, capture efficiencies with the DNA oligomer were significantly greater than with the PNA clamp and PNA oligomer. Recovery and detection efficiencies for target DNA concentrations of ≥100 pg were generally >20% but depended upon the specific probe, solution background, and salt condition. The DNA probe had a lower absolute detection limit of 100 fg of target (830 zM [1 zM = 10−21 M]) in high-salt buffer. In the absence of exogenous DNA (e.g., soil background), neither the bis-PNA nor the PNA oligomer achieved the same absolute detection limit even under a more favorable low-salt hybridization condition. In the presence of a soil background, however, both PNA probes provided more sensitive absolute purification and detection (830 zM) than the DNA oligomer. In varied environmental samples, the rank order for capture probe performance in high-salt buffer was DNA > PNA > clamp. Recovery of 16S rRNA from environmental samples mirrored quantitative results for DNA target recovery, with the DNA oligomer generating more positive results than either the bis-PNA or PNA oligomer, but PNA probes provided a greater incidence of detection from environmental samples that also contained a higher concentration of nontarget DNA and RNA. Significant interactions between probe type and environmental sample indicate that the most efficacious capture system depends upon the particular sample type (and background nucleic acid concentration), target (DNA or RNA), and detection objective.

Gelling Properties of Heat-Denatured β-Lactoglobulin Aggregates in a High-Salt Buffer

2002 ◽  
Vol 50 (10) ◽  
pp. 2987-2992 ◽  
Author(s):  
Manee Vittayanont ◽  
James F. Steffe ◽  
Stanley L. Flegler ◽  
Denise M. Smith
Keyword(s):  
High Salt ◽  
Gelling Properties ◽  
High Salt Buffer ◽  
Β Lactoglobulin

scholarly journals Transplantation of Quail Collagen-tailed Acetylcholinesterase Molecules Onto the Frog Neuromuscular Synapse

1997 ◽  
Vol 136 (2) ◽  
pp. 367-374 ◽  
Author(s):  
Richard L. Rotundo ◽  
Susana G. Rossi ◽  
Lili Anglister
Keyword(s):  
Basal Lamina ◽  
Binding Sites ◽  
Acetylcholine Receptors ◽  
Neuromuscular Junctions ◽  
Specific Binding ◽  
Neuromuscular Synapse ◽  
High Salt ◽  
Specific Binding Sites ◽  
Parking Lot ◽  
High Salt Buffer

The highly organized pattern of acetylcholinesterase (AChE) molecules attached to the basal lamina of the neuromuscular junction (NMJ) suggests the existence of specific binding sites for their precise localization. To test this hypothesis we immunoaffinity purified quail globular and collagen-tailed AChE forms and determined their ability to attach to frog NMJs which had been pretreated with high-salt detergent buffers. The NMJs were visualized by labeling acetylcholine receptors (AChRs) with TRITC-α-bungarotoxin and AChE by indirect immunofluorescence; there was excellent correspondence (>97%) between the distribution of frog AChRs and AChE. Binding of the exogenous quail AChE was determined using a speciesspecific monoclonal antibody. When frog neuromuscular junctions were incubated with the globular G4/G2 quail AChE forms, there was no detectable binding above background levels, whereas when similar preparations were incubated with the collagen-tailed A12 AChE form >80% of the frog synaptic sites were also immunolabeled for quail AChE attached. Binding of the A12 quail AChE was blocked by heparin, yet could not be removed with high salt buffer containing detergent once attached. Similar results were obtained using empty myofiber basal lamina sheaths produced by mechanical or freeze-thaw damage. These experiments show that specific binding sites exist for collagen-tailed AChE molecules on the synaptic basal lamina of the vertebrate NMJ and suggest that these binding sites comprise a “molecular parking lot” in which the AChE molecules can be released, retained, and turned over.

scholarly journals High-Voltage and High-Salt Buffer Facilitates Electroporation of Human Aortic Smooth-Muscle Cells

BioTechniques ◽  
1998 ◽  
Vol 24 (4) ◽  
pp. 590-592 ◽  
Author(s):  
Chang-Ning Yan ◽  
Fengzhi Li ◽  
Cam Patterson ◽  
Marschall S. Runge
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
High Voltage ◽  
Muscle Cells ◽  
High Salt ◽  
Aortic Smooth Muscle Cells ◽  
Aortic Smooth Muscle ◽  
High Salt Buffer

High Salt Buffer

2019 ◽  
Vol 2019 (2) ◽  
pp. pdb.rec104083
Keyword(s):  
High Salt ◽  
High Salt Buffer
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