Prostaglandins alter methacholine-induced secretion in ferret in vitro trachea

1990 ◽  
Vol 258 (2) ◽  
pp. L75-L80 ◽  
Author(s):  
M. E. Deffebach ◽  
H. Islami ◽  
A. Price ◽  
S. E. Webber ◽  
J. G. Widdicombe
Keyword(s):  
Bovine Serum Albumin ◽  
Bovine Serum ◽  
Specific Marker ◽  
Albumin Concentration ◽  
Organ Bath ◽  
Cell Secretion ◽  
Serous Cell ◽  
Dose Dependent ◽  
Tracheal Secretion

The ferret trachea was mounted in an organ bath containing Krebs-Henseleit solution with additional bovine serum albumin (BSA). Tracheal secretions were collected and analyzed for albumin, and lysozyme, a specific marker of serous cell secretion. The total secretion volume and output and concentrations of albumin and lysozyme were calculated. Secretion was stimulated with methacholine (20 microM) (Mch), and the effects of the prostaglandins PGD2, PGE1, and PGF2 alpha on methacholine-induced secretion were studied. All responses were dose dependent. PGF2 alpha at 10(-5) M increased the volume of Mch-stimulated secretion twofold, the lysozyme output sixfold, and concentration over threefold, while decreasing the albumin transport by one-half. PGD2 at 10(-5) M reduced Mch-induced secretion volume to 75% control, increased albumin transport to 135%, without affecting lysozyme secretion. PGE1 at 10(-5) M increased Mch-stimulated albumin transport and concentration over twofold, decreased lysozyme release to less than one-third of control, and had no effect on secretion volume. PGE1 caused the albumin concentration to exceed that of the outer bath, indicating active transport. We conclude that prostaglandins selectively alter tracheal secretion induced by cholinergic stimuli.

Transport of albumin by the rabbit trachea in vitro

1990 ◽  
Vol 68 (2) ◽  
pp. 726-730 ◽  
Author(s):  
A. M. Price ◽  
S. E. Webber ◽  
J. G. Widdicombe
Keyword(s):  
Bovine Serum Albumin ◽  
Sodium Cyanide ◽  
Organ Bath ◽  
Submucosal Gland ◽  
Cell Secretion ◽  
Mucosal Transport ◽  
Submucosal Glands ◽  
Serous Cell ◽  
Fluorescent Dextran

The rabbit whole trachea was mounted in vitro in an organ bath containing Krebs-Henseleit (KH) solution. When the trachea was air filled there was no resting secretion and none was induced by methacholine (0.02 mM). Histology showed that the trachea has very few submucosal glands. When the trachea was filled with KH, with fluorescent bovine serum albumin in the surrounding KH solution, the rate of transport of albumin into the lumen was measured. Methacholine (0.02 mM) and phenylephrine (0.1 mM) more than doubled the output of albumin, and albuterol (0.1 mM) increased it more than fourfold. Cooling the preparation to 4 degrees C decreased the spontaneous output of albumin to less than one-half control and abolished the increase in output due to albuterol. Addition of sodium cyanide (1 mM) to the preparation abolished the increase in albumin transport due to albuterol. Serosal-to-mucosal transport of fluorescent dextran (mol wt 70,000) was less than one-third that of albumin and was not enhanced by methacholine, phenylephrine, or albuterol. Lysozyme output, an index of serous cell secretion, was barely detectable in controls and was not enhanced by any of the drugs. We conclude that the rabbit trachea has no measurable submucosal gland secretion and that it can actively transport albumin into the lumen via the epithelium. The transport rate is enhanced by methacholine, phenylephrine, and especially by albuterol.

A Precipitin-like Reaction of the Hemolymph of the Lobster Homarus americanus

1969 ◽  
Vol 26 (5) ◽  
pp. 1392-1397 ◽  
Author(s):  
James E. Stewart ◽  
Diane M. Foley
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Serum Proteins ◽  
Homarus Americanus ◽  
Test Period ◽  
Fluorescent Material

The levels of fluorescent material in the hemolymph of lobsters injected with serum proteins from lobster hemolymph labelled with fluorescein remained relatively constant over a 6-day test period; the levels in lobsters injected with bovine serum albumin labelled with fluorescein declined rapidly. A precipitin-like reaction was observed when lobster hemolymph serum was titrated with bovine serum albumin in vitro.

Preparation and in vitro photodynamic activities of novel axially substituted silicon (IV) phthalocyanines and their bovine serum albumin conjugates

2006 ◽  
Vol 16 (9) ◽  
pp. 2450-2453 ◽  
Author(s):  
Xiong-Jie Jiang ◽  
Jian-Dong Huang ◽  
Yu-Jiao Zhu ◽  
Fen-Xiang Tang ◽  
Dennis K.P. Ng ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

Amuchina Gel Xgerm hand rub in vitro virucidal activity against SARS-CoV-2

2021 ◽  
Author(s):  
Alessandra Capezzone de Joannon ◽  
Angela Testa ◽  
Natalie Falsetto ◽  
Michela Procaccini ◽  
Lorella Ragni
Keyword(s):  
Detection Limit ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Virucidal Activity ◽  
European Standard ◽  
Enveloped Viruses ◽  
Prevention Measure ◽  
Study Product

Aim: Ethanol is highly effective at inactivating enveloped viruses, including SARS-CoV-2. The aim of this study is to evaluate the virucidal activity of Amuchina Gel Xgerm (74% ethanol) against SARS-CoV-2, according to the European Standard EN14476:2013+A2:2019. Materials & methods: Virucidal activity of the study product was evaluated against SARS-CoV-2 strain USAWA1/2020 in suspension, in the presence of 0.3 g/l of bovine serum albumin. Results: The log10 reduction of SARS-CoV-2 in the presence of bovine serum albumin was ≥4.11 ± 0.12 after 30 s of exposure to the study product (80% dilution). Cytotoxicity was observed in the 100 dilution, affecting the detection limit by 1 log10. Conclusion: Virucidal activity against SARS-CoV-2 supports the effectiveness of this alcohol-based formulation as a prevention measure for COVID-19 illness.

scholarly journals In-vitro displacement interaction of atenolol and amlodipine on binding with bovine serum albumin when co-administered

2008 ◽  
Vol 2 (1) ◽  
Author(s):  
Md Ashraful Alam ◽  
Md Abdul Awal ◽  
Mahbub Mostofa ◽  
Md Kamrul Islam ◽  
Nusrat Subhan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

Bovine serum albumin (BSA) can replace patient serum as a protein source in an in vitro fertilization (IVF) program

1989 ◽  
Vol 6 (3) ◽  
pp. 164-167 ◽  
Author(s):  
Claudio A. Benadiva ◽  
Barbara Kuczynski-Brown ◽  
Tobi G. maguire ◽  
Luigi Mastroianni ◽  
George L. Flickinger
Keyword(s):  
In Vitro Fertilization ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Source ◽  
Vitro Fertilization

In Vitro Study of the Binding of Taxifolin to Bovine Serum Albumin and the Influence of Common Ions on the Binding

2010 ◽  
Vol 39 (4) ◽  
pp. 482-494 ◽  
Author(s):  
Xiaolei Shi ◽  
Xuwen Li ◽  
Yantao Sun ◽  
Wei Wei ◽  
Ruijie Yang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
In Vitro Study ◽  
Vitro Study

scholarly journals Clearance and binding of native and defucosylated lactoferrin

1983 ◽  
Vol 212 (2) ◽  
pp. 249-257 ◽  
Author(s):  
M J Imber ◽  
S V Pizzo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Binding ◽  
Gel Filtration ◽  
Peritoneal Macrophages ◽  
Mononuclear Phagocyte ◽  
Stable Complex

These studies explore the role of carbohydrate recognition systems and the direct involvement of terminal alpha 1-3-linked fucose in the clearance of lactoferrin from the murine circulation and in the specific binding of lactoferrin to receptors on murine peritoneal macrophages. As previously reported, radiolabelled lactoferrin cleared very rapidly (t1/2 less than 1 min) after intravenous injection into mice. However, competing levels of ligands specific for the hepatic galactose receptor (asialo-orosomucoid), the hepatic fucose receptor (fucosyl-bovine serum albumin), and the mononuclear-phagocyte system pathway recognizing mannose, N-acetylglucosamine and fucose (mannosyl-, N-acetylglucosaminyl- and fucosyl-bovine serum albumin) did not block radiolabelled lactoferrin clearance in vivo or binding to mouse peritoneal macrophage monolayers in vitro. Almond emulsin alpha 1-3-fucosidase was used to prepare defucosylated lactoferrin in which 88% of the alpha 1-3-linked fucose was hydrolysed. No difference in clearance or receptor binding was observed between radiolabelled native and defucosylated lactoferrin. Fucoidin, a fucose-rich algal polysaccharide, completely inhibits the clearance in vivo and macrophage binding in vitro of lactoferrin. This effect, however, is probably not the result of competition for binding to the fucose receptor, since gel-filtration studies demonstrated formation of a stable complex between lactoferrin and fucoidin. The present results indicate that the lactoferrin-clearance pathway is distinct from several pathways mediating glycoprotein clearance through recognition of terminal galactose, fucose, N-acetylglucosamine or mannose. Furthermore, alpha 1-3-linked fucose on lactoferrin is not essential for lactoferrin clearance in vivo or specific binding to macrophage receptors in vitro.

Study of in vitro interaction between tetrabromobisphenol A and bovine serum albumin by fluorescence spectroscopy

2011 ◽  
Vol 30 (12) ◽  
pp. 2697-2700 ◽  
Author(s):  
Yingxin Wu ◽  
Yan Qian ◽  
Hao Cui ◽  
Xiaomin Lai ◽  
Xianchuan Xie ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Tetrabromobisphenol A ◽  
In Vitro Interaction
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