The adsorption of bovine serum albumin at the stainless-steel/aqueous solution interface

1984 ◽  
Vol 98 (1) ◽  
pp. 138-143 ◽  
Author(s):  
H VANENCKEVORT ◽  
D DASS ◽  
A LANGDON
Keyword(s):  
Aqueous Solution ◽  
Stainless Steel ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Solution Interface

Interaction of Bovine Serum Albumin and Lysozyme with Stainless Steel Studied by Time-of-Flight Secondary Ion Mass Spectrometry and X-ray Photoelectron Spectroscopy

Langmuir ◽  
2012 ◽  
Vol 28 (47) ◽  
pp. 16306-16317 ◽  
Author(s):  
Yolanda S. Hedberg ◽  
Manuela S. Killian ◽  
Eva Blomberg ◽  
Sannakaisa Virtanen ◽  
Patrik Schmuki ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Stainless Steel ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Photoelectron Spectroscopy ◽  
Bovine Serum ◽  
Secondary Ion Mass Spectrometry ◽  
Time Of Flight ◽  
X Ray ◽  
Secondary Ion

Exploration of interactions between decyl-β-d-glucopyranoside and bovine serum albumin in aqueous solution

RSC Advances ◽  
2016 ◽  
Vol 6 (24) ◽  
pp. 19700-19706 ◽  
Author(s):  
Gongke Wang ◽  
Huimin Hou ◽  
Ye Chen ◽  
Changling Yan ◽  
Guangyue Bai ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Surface Tension ◽  
Steady State ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Absorption Spectroscopy ◽  
Bovine Serum ◽  
Aqueous Media ◽  
Steady State Fluorescence

The interactions between decyl-β-d-glucopyranoside (DG) and bovine serum albumin (BSA), in aqueous media, were investigated through the use of surface tension, steady-state fluorescence, and UV-vis absorption spectroscopy measurements.

scholarly journals Thermally induced conformational changes and protein–protein interactions of bovine serum albumin in aqueous solution under different pH and ionic strengths as revealed by SAXS measurements

2017 ◽  
Vol 19 (26) ◽  
pp. 17143-17155 ◽  
Author(s):  
Dmitry Molodenskiy ◽  
Evgeny Shirshin ◽  
Tatiana Tikhonova ◽  
Andrey Gruzinov ◽  
Georgy Peters ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Changes ◽  
Interaction Potential ◽  
Protein Interactions ◽  
Bovine Serum ◽  
Protein Protein Interactions ◽  
Thermally Induced ◽  
Before And After

Temperature-induced oligomerization of albumin before and after protein melting was studied using SAXS and interpreted in terms of interaction potential.

Sterilization of Heat-Resistant Instruments With Infrared Radiation

2002 ◽  
Vol 23 (7) ◽  
pp. 393-396 ◽  
Author(s):  
Victor Hugo Mata-Portuguez ◽  
Leonor Sánchez Pérez ◽  
Enrique Acosta-Gío
Keyword(s):  
Stainless Steel ◽  
Bacillus Subtilis ◽  
Bovine Serum Albumin ◽  
Infection Control ◽  
Serum Albumin ◽  
Infrared Radiation ◽  
Bovine Serum ◽  
Culture Collection ◽  
Culture Negative ◽  
D Value

Objective:To evaluate the lethality profile of an infrared radiation (IR) prototype sterilizer.Method:Simulated use and D value tests were conducted with Bacillus subtilis spores American Type Culture Collection–9372. A spore suspension (1.06 ± 0.03 × 106) in 5% bovine serum albumin was air dried on stainless steel instruments. IR cycles were completed and the instruments were immersed in tryptic soy broth for 120 hours at 37°C. Direct enumeration of survivors was performed to evaluate IR death. Instrument loads contained carriers laden with spores (1.06 ± 0.3 × 106). The spores were seeded on tryptic soy agar and survivors were counted after 120 hours of incubation at 37°C.Results:All instruments exposed to IR (n = 50) were culture negative. In contrast, all unprocessed instruments (n = 30) showed B. subtilis growth. The prototype's D value was 0.56, and the death rate's slope was -1.76 (r = -0.99741; P < .0001). The 10-6 sterility assurance level was reached after 8 minutes and 40 seconds of exposure, from cold start.Conclusions:IR destroys B. subtilis spores. Instrument sterilization with IR may provide another technology for infection control.

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