Matches in SemOpenAlex for { <https://semopenalex.org/work/W1990793611> ?p ?o ?g. }
Showing items 1 to 100 of
100
with 100 items per page.
- W1990793611 endingPage "478" @default.
- W1990793611 startingPage "473" @default.
- W1990793611 abstract "We developed a new method (dropping time method, DTM) to investigate the wettability of a surface of a protein layer adsorbed on glass plates in aqueous solution. However, the previous setup of DTM can only be utilized for optically transparent materials. In this study, we have extended the method to optically nontransparent materials such as hydroxyapatite plates. DTM is based on measuring the dropping time of a liquid film along a protein-covered surface when this surface is instantaneously vertically removed from the protein solution. The intensity of the reflected light beam depends on the presence of a liquid film on the surface. This allows to estimate the movement of the liquid film along the sorbent surface. Thus, the extended DTM can be used for determining the wettability of optically nontransparent solid plates. The adsorption behavior of four proteins (albumin, lysozyme, beta-lactoglobulin, ovalbumin) on a hydrophobic hydroxyapatite plate in water was studied by this method. When adsorbed from a protein solution of high concentration, the surfaces of adsorbed proteins, except ovalbumin, were fairly hydrophilic; this hydrophilicity was already attained at the initial stage of the adsorption process. The surface of ovalbumin on hydroxyapatite was more hydrophobic than those of the other proteins, and the hydrophilicity increased with the protein adsorption process. At low protein concentration, the hydrophilicity increased in the course of the adsorption process. The change in hydrophilicity with time depends on the kind of protein. Hen's egg lysozyme is more hydrophilic and the time to reach saturation is shorter than for the other proteins. The processes of increasing hydrophilicity of the surface of human serum albumin, beta-lactoglobulin and ovalbumin are similar. However, for beta-lactoglobulin hydrophobicity at adsorption saturation is stronger than for human serum albumin and ovalbumin. Thus, using DTM it is shown that the hydrophilicity of the surface of adsorbed protein on hydroxyapatite depends strongly on the kind of protein." @default.
- W1990793611 created "2016-06-24" @default.
- W1990793611 creator A5000000874 @default.
- W1990793611 creator A5013971568 @default.
- W1990793611 creator A5021984114 @default.
- W1990793611 creator A5055388455 @default.
- W1990793611 date "1999-01-01" @default.
- W1990793611 modified "2023-09-23" @default.
- W1990793611 title "Measurements of the Wettability of Protein–Covered Hydroxyapatite Surfaces" @default.
- W1990793611 cites W1994342473 @default.
- W1990793611 cites W2003714897 @default.
- W1990793611 cites W2093395937 @default.
- W1990793611 cites W2144798802 @default.
- W1990793611 cites W2170236036 @default.
- W1990793611 doi "https://doi.org/10.1159/000016554" @default.
- W1990793611 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10529534" @default.
- W1990793611 hasPublicationYear "1999" @default.
- W1990793611 type Work @default.
- W1990793611 sameAs 1990793611 @default.
- W1990793611 citedByCount "15" @default.
- W1990793611 countsByYear W19907936112012 @default.
- W1990793611 countsByYear W19907936112013 @default.
- W1990793611 countsByYear W19907936112015 @default.
- W1990793611 countsByYear W19907936112018 @default.
- W1990793611 countsByYear W19907936112022 @default.
- W1990793611 crossrefType "journal-article" @default.
- W1990793611 hasAuthorship W1990793611A5000000874 @default.
- W1990793611 hasAuthorship W1990793611A5013971568 @default.
- W1990793611 hasAuthorship W1990793611A5021984114 @default.
- W1990793611 hasAuthorship W1990793611A5055388455 @default.
- W1990793611 hasConcept C114614502 @default.
- W1990793611 hasConcept C127413603 @default.
- W1990793611 hasConcept C134514944 @default.
- W1990793611 hasConcept C150394285 @default.
- W1990793611 hasConcept C159985019 @default.
- W1990793611 hasConcept C178790620 @default.
- W1990793611 hasConcept C184651966 @default.
- W1990793611 hasConcept C185592680 @default.
- W1990793611 hasConcept C192562407 @default.
- W1990793611 hasConcept C203014093 @default.
- W1990793611 hasConcept C2776946954 @default.
- W1990793611 hasConcept C2776966407 @default.
- W1990793611 hasConcept C2777899863 @default.
- W1990793611 hasConcept C2779227376 @default.
- W1990793611 hasConcept C33923547 @default.
- W1990793611 hasConcept C42360764 @default.
- W1990793611 hasConcept C43617362 @default.
- W1990793611 hasConcept C55493867 @default.
- W1990793611 hasConcept C6556556 @default.
- W1990793611 hasConcept C86803240 @default.
- W1990793611 hasConcept C86807702 @default.
- W1990793611 hasConcept C88001094 @default.
- W1990793611 hasConcept C8891405 @default.
- W1990793611 hasConcept C9930424 @default.
- W1990793611 hasConceptScore W1990793611C114614502 @default.
- W1990793611 hasConceptScore W1990793611C127413603 @default.
- W1990793611 hasConceptScore W1990793611C134514944 @default.
- W1990793611 hasConceptScore W1990793611C150394285 @default.
- W1990793611 hasConceptScore W1990793611C159985019 @default.
- W1990793611 hasConceptScore W1990793611C178790620 @default.
- W1990793611 hasConceptScore W1990793611C184651966 @default.
- W1990793611 hasConceptScore W1990793611C185592680 @default.
- W1990793611 hasConceptScore W1990793611C192562407 @default.
- W1990793611 hasConceptScore W1990793611C203014093 @default.
- W1990793611 hasConceptScore W1990793611C2776946954 @default.
- W1990793611 hasConceptScore W1990793611C2776966407 @default.
- W1990793611 hasConceptScore W1990793611C2777899863 @default.
- W1990793611 hasConceptScore W1990793611C2779227376 @default.
- W1990793611 hasConceptScore W1990793611C33923547 @default.
- W1990793611 hasConceptScore W1990793611C42360764 @default.
- W1990793611 hasConceptScore W1990793611C43617362 @default.
- W1990793611 hasConceptScore W1990793611C55493867 @default.
- W1990793611 hasConceptScore W1990793611C6556556 @default.
- W1990793611 hasConceptScore W1990793611C86803240 @default.
- W1990793611 hasConceptScore W1990793611C86807702 @default.
- W1990793611 hasConceptScore W1990793611C88001094 @default.
- W1990793611 hasConceptScore W1990793611C8891405 @default.
- W1990793611 hasConceptScore W1990793611C9930424 @default.
- W1990793611 hasIssue "6" @default.
- W1990793611 hasLocation W19907936111 @default.
- W1990793611 hasLocation W19907936112 @default.
- W1990793611 hasOpenAccess W1990793611 @default.
- W1990793611 hasPrimaryLocation W19907936111 @default.
- W1990793611 hasRelatedWork W1583995776 @default.
- W1990793611 hasRelatedWork W170649201 @default.
- W1990793611 hasRelatedWork W1955134310 @default.
- W1990793611 hasRelatedWork W2025522099 @default.
- W1990793611 hasRelatedWork W2066683175 @default.
- W1990793611 hasRelatedWork W2081942298 @default.
- W1990793611 hasRelatedWork W2302990881 @default.
- W1990793611 hasRelatedWork W2369329827 @default.
- W1990793611 hasRelatedWork W3151576315 @default.
- W1990793611 hasRelatedWork W4302013047 @default.
- W1990793611 hasVolume "33" @default.
- W1990793611 isParatext "false" @default.
- W1990793611 isRetracted "false" @default.
- W1990793611 magId "1990793611" @default.
- W1990793611 workType "article" @default.