Visualization of native chromatin fibers in different embedding media

1978 ◽  
Vol 36 (2) ◽  
pp. 222-223
Author(s):  
Sebastian Muñoz-Guerra ◽  
Juan A. Subirana
Keyword(s):  
Fine Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble ◽  
Critical Importance ◽  
Thin Sections ◽  
Glycol Methacrylate ◽  
Embedding Medium ◽  
Holothuria Polii

The influence of the embedding medium is of critical importance in the observation of nucleoprotein structures in thin sections. The use of conventional epoxi media requires dehydratation, impregnation and subsequent polymerization, which may produce drastic alterations in the fine structure of chromatin. The use of water soluble embedding media may lead to improvements in the preservation of ultrastructure. In this paper we explore the differences which may be detected in nucleohistone fibers embedded in different media.Spermatozoa from Holothuria polii were subjected to moderate lysis in either 0.15M NaCl, ImM Tris-HCl, 0.4mM CaCl2, pH 8.0 (a) or 0.25M sucrose, 0.4mM CaCl2 (b) and then fixed by addition of 2 % glutaralde- hyde. Embedding was carried out as described in the literature in the following media: araldite-epon mixture (AREPO), glycol methacrylate (GMA, 1), hydroxipropyl methacrylate (HPMA, 2) and bovine serum albumin (BSA, 3) or histones.

scholarly journals Antibody labeling of thin sections of skeletal muscle with specific antibodies: a comparison of bovine serum albumin (BSA) embedding and ultracryomicrotomy.

1980 ◽  
Vol 28 (9) ◽  
pp. 969-978 ◽  
Author(s):  
G W Griffiths ◽  
B M Jockusch
Keyword(s):  
Skeletal Muscle ◽  
Fine Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Additional Advantage ◽  
Thin Sections ◽  
Quantitative Estimates ◽  
Semithin Sections ◽  
Antibody Labeling

Bovine serum albumin (BSA) embedding and ultracryomicrotomy were used to prepare thin sections of glutaraldehyde-fixed skeletal muscle; these were then treated with antibodies against alpha-actinin, myosin, and actin. Three criteria were then used to compare these two techniques: 1) The preservation of fine structure; 2) the specificity of labeling with antibodies and 3) the amount of antibody bound to a particular antigen. Fine structure was better preserved using ultracryomicrotomy. Both techniques, under optimal conditions, gave specific labeling of muscle components. The amount of antibody bound was higher for BSA sections than for frozen sections. The conclusion is that, while ultracryomicrotomy gives superior qualitative results, the most reliable quantitative estimates would be obtained by using both methods together. Ultracryomicrotomy has the additional advantage that semithin sections can be visualized by immunofluorescence.

Preparation and Application as Biosensor of Water-Soluble Conjugated Polyelectrolyte

2013 ◽  
Vol 538 ◽  
pp. 301-304
Author(s):  
Yi Ping Zhong ◽  
Rui Bin Hong ◽  
Bin Bin Yin ◽  
Ping Liu ◽  
Wen Ji Deng
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble ◽  
Conjugated Polyelectrolyte ◽  
Sodium Sulfonate ◽  
Vis Spectroscopy

The water-soluble conjugated polyelectrolyte, poly[3-(1′-propyloxy-3′-sodium sulfonate) thiophene] (PTH-n3-SO3Na), was prepared. The interaction between the PTH-n3-SO3Na and bovine serum albumin (BSA) was investigated using UV-vis spectroscopy. It was found that the PTH-n3-SO3Na could be used as biosensor to detect BSA.

scholarly journals Spectroscopic Studies on the Interaction of a Water-Soluble Cationic Porphyrin with Bovine Serum Albumin

2013 ◽  
Vol 36 (1-2) ◽  
pp. 21-26 ◽  
Author(s):  
Hamid Dezhampanah ◽  
Abdol-Khalegh Bordbar ◽  
Yadolahe Khodadusdt
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molecular Conformation ◽  
Fluorescence Emission ◽  
Water Soluble ◽  
Aggregate Formation ◽  
Cationic Porphyrin ◽  
Porphyrin Complex ◽  
Induced Aggregation

The interaction of a water-soluble cationic porphyrin, Cobalt(III) 5, 10, 15, 20-tetrakis (1-methylpyridinium-4-yl) porphyrin [Co(III)TMPyP], with bovine serum albumin (BSA) has been studied in 1 mM phosphate buffer pH 7.0 containing 5 mM NaCl by UV-vis absorption, resonance light scattering (RLS) and fluorescence spectroscopies at 25°C. The results of RLS studies represent no aggregate formation of porphyrin in the surface of BSA and low tendency of this porphyrin for aggregate formation.The binding of porphyrin complex to BSA quenches fluorescence emission of BSA via a dynamic mechanism and the quenching process obeys a linear Stern-Volmer relationship. The values of Stern-Volmer constants, KSV, was determined nearly 105M−1, that depend on BSA concentration. The average aggregation number of BSA calculated from the analysis of fluorescence quenching data indicates that absence of any porphyrin induced aggregation of BSA due to its interaction with porphyrin complex. The binding of Co(III) TMPyP had no obvious effect on the molecular conformation of the protein. Electrostatic force played an important role in the binding due to the opposite charges on porphyrin and the protein.

Synthesis of Water-Soluble Red-Emitting Thienyl-BODIPYs and Bovine Serum Albumin Labeling

2014 ◽  
Vol 20 (5) ◽  
pp. 1252-1257 ◽  
Author(s):  
Arnaud Poirel ◽  
Pascal Retailleau ◽  
Antoinette De Nicola ◽  
Raymond Ziessel
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Water Soluble
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