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1 seins with more stable complexes formed with alpha-casein.
2 ified 21 out of 22 phosphorylation sites for alpha-casein.
3 pplied to tryptic digests of beta-casein and alpha-casein.
4 one generated from the tryptic digestion of alpha-casein.
5 's catalytic activities after an addition of alpha-casein.
6 and stimulated by unfolded proteins such as alpha-casein.
7 type levels, by the Ms-Lon substrate protein alpha-casein.
8 ng from addition of the nonchaperone protein alpha-casein.
9 se activities were only stimulated weakly by alpha-casein.
10 ith overall binding constants of K(retinol-)(alpha)(-caseins)=1.21 (+/-0.4)x10(5) M(-1) and K(retinol
11 1 (+/-0.5)x10(5) M(-1) and K(retinoic acid-)(alpha)(-caseins)=6.2 (+/-0.6)x10(4) M(-1) and K(retinoic
12 o identify and sequence phosphopeptides from alpha-casein, a milk-derived protein possessing up to ni
13 tion of sodium caseinate (NaCN) and purified alpha-casein (alphas-CN) with an Aspergillus niger deriv
15 lity of AI-ETD in localizing phosphosites in alpha-casein, an approximately 23.5 kDa phosphoprotein t
16 showed that PrkA is indeed able to hydrolyze alpha-casein, an exogenous substrate of Lon proteases, i
17 lecules per protein (n) was 1.5 (+/-0.1) for alpha-casein and 1.0 (+/-0.1) for beta-casein, while 1 m
19 pH of aqueous samples of the phosphoprotein alpha-casein and comparing this result with dephosphoryl
20 aperones), as well as small proteins such as alpha-casein and detergents acting as "artificial chaper
24 ition of the reaction was <=20 and <=68% for alphas-casein and whey protein concentrate respectively.
25 in E. coli samples, BSA, beta-lactoglobulin, alpha-casein, and alpha-lactalbumin, was achieved, using
26 from complex peptide mixtures of ovalbumin, alpha-casein, and beta-casein digests were also achieved
27 d was developed for allergens analysis using alpha-casein as the biomarker for cow's milk detection,
28 or demonstrated good selectivity towards the alpha-casein as the target analyte and adequate recoveri
30 e its higher content of proline, compared to alpha-casein, beta-casein did not always have a higher a
31 des from tryptic digest of standard protein (alpha-casein, beta-casein, and commercially available ca
32 amide I band of alpha-synuclein, phosvitin, alpha-casein, beta-casein, and the non-A beta component
33 h as the higher total protein, total casein, alpha-casein, beta-casein, kappa-casein and alpha-tocoph
35 ed when carboxymethylated bovine albumin and alpha-casein, considered to mimic proteins with extended
39 and the hydrophobicity profiles we show that alpha-casein has a pair of helices that have similar seq
40 sted from a complex mixture containing 7% of alpha-casein identified 21 out of 22 phosphorylation sit
41 bacterial culture was mixed with the BODIPY-alpha-casein in a buffer of an appropriate pH and the de
42 idase activities were stimulated strongly by alpha-casein in the case of Ms-Lon but weakly by alpha-c
45 ptides identified in the acid hydrolysate of alpha casein increased by 45% and the number of peptides
48 The gold sensor chip was used to immobilise alpha-casein-polyclonal antibody using EDC/NHS coupling
53 3 triphosphopeptides were identified in the alpha-casein sample, while 19 mono-, 8 di-, 4 tri-, and
54 comparing this result with dephosphorylated alpha-casein, spectral variations in phosphate stretch b
55 Measured phosphopeptide fold-changes from alpha-casein spiked into wild-type zebrafish lysate back
56 rocyanidin A1 displayed a higher affinity to alpha-casein than the supposedly more flexible B-type di
57 EVSLNSGYY, barley; PGTAVFK, soybean; TTMPLW, alpha-casein; VHLPP, alpha-zein) and the six alanine sub
59 proteoforms of cytochrome C, myoglobin, and alpha-casein were separated and resolved with high repro
60 se during the NH2-terminal aminoacylation of alpha-casein, whereas Val-tRNAVal-1 (UAC), Val-tRNAMetm
61 omparing the structures of the non-chaperone alpha-casein (which has no sequence similarity with the