Zobrazeno 1 - 3
of 3
pro vyhledávání: '"N V, Grinberg"'
Publikováno v:
Die Nahrung. 42(3-4)
Spectroscopic and thermodynamic studies of holo-alpha-lactalbumin folding show that in hydro-ethanolic media this protein structure is subjected to at least three distinct transitions induced by ethanol. As observed by spectrofluorescence and circula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8440e6caeba96e32d7add337b1bc1624
https://pubmed.ncbi.nlm.nih.gov/9739563
https://pubmed.ncbi.nlm.nih.gov/9739563
Publikováno v:
Die Nahrung. 42(3-4)
Interactions of food proteins--beta-lactoglobulin (BLG), bovine serum albumin (BSA) und ovalbumin (OA)--with vanillin and effect of thermal denaturation of the proteins on vanillin binding were studies by US-VIS spectrophotometry. This method has its
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::107ab43d0e08faba7a34f4b4b358192d
https://pubmed.ncbi.nlm.nih.gov/9739564
https://pubmed.ncbi.nlm.nih.gov/9739564
Publikováno v:
Biopolymers. 46(4)
Conformational transitions of holo-alpha-lactalbumin in a hydro-ethanolic cosolvent system was studied by spectrofluorescence, CD in near- and far-uv regions, and high-sensitivity differential scanning calorimetry. Experimental results allow us to pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::7f2e5f3a49a61be2dbf5f9b68ac2a0e0
https://pubmed.ncbi.nlm.nih.gov/9715667
https://pubmed.ncbi.nlm.nih.gov/9715667