2008
DOI: 10.1590/s0101-20612008000400032
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Composition and physicochemical properties of two protein fractions of bovine blood serum

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Cited by 13 publications
(7 citation statements)
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References 29 publications
(22 reference statements)
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“…Other studies evaluated the amino acids profile of RBPC showing some variations, probably, due to the protein extraction procedure employed (TANG et al, 2003;HAN et al, 2015). Comparing the RBPC amino acids profile with BSA, lower amino acids content was observed for RBPC, an expected condition, since the BSA is a protein of high biological value (PRATA & SGARBIERI, 2008).…”
Section: Rbpc Composition and Colormentioning
confidence: 99%
“…Other studies evaluated the amino acids profile of RBPC showing some variations, probably, due to the protein extraction procedure employed (TANG et al, 2003;HAN et al, 2015). Comparing the RBPC amino acids profile with BSA, lower amino acids content was observed for RBPC, an expected condition, since the BSA is a protein of high biological value (PRATA & SGARBIERI, 2008).…”
Section: Rbpc Composition and Colormentioning
confidence: 99%
“…As a result, one could speculate that charge transfer from the ligand (BSA) to the metal (Au) core [ligand to metal charge transfer (LMCT)] through the Au−S bonds and direct donation of delocalized electrons of electron rich atoms or groups of the ligand to the metal core could be a plausible reason for the luminescent properties of the GNC. As cysteine is one of the amino acids present in BSA 36 that contains a SH group, upon synthesis of the GNC this SH group forms the well-known gold−sulfur interface and LMCT takes place through the Au−S bond. The quantum yield (QY) of 6%, the fluorescence lifetime of 5.4 ns (Figure 2d), and the potential low toxicity 30 of the GNC allow for its use as a fluorescent probe for SRM imaging of lysosomes in HeLa cells.…”
mentioning
confidence: 99%
“…When pH increases from 9 to 11, the −NH þ 3 on the side chains of lysine convert to −NH 2 , further increasing the labeling efficiency. According to Table 1, at pH 11, the increase in labeling efficiency compared with pH 9 is greater than the content of lysine in BSA, which is about 12% as reported [42]. This excessive increment may be attributed to two possibilities.…”
Section: Verification Of Improved Labeling Efficiency By Bsamentioning
confidence: 75%