ライフサイエンスコーパス: alpha-casein

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

14 Among the casein components, alphas-casein (alphas-CAS) is considered the major aller

15 lity of AI-ETD in localizing phosphosites in alpha-casein, an approximately 23.5 kDa phosphoprotein t

16 lecules per protein (n) was 1.5 (+/-0.1) for alpha-casein and 1.0 (+/-0.1) for beta-casein, while 1 m

17 ns) and several monomeric flavan-3-ols, with alpha-casein and beta-casein, were investigated.

18 pH of aqueous samples of the phosphoprotein alpha-casein and comparing this result with dephosphoryl

19 aperones), as well as small proteins such as alpha-casein and detergents acting as "artificial chaper

20 Digests of alpha-casein and ss-casein were analyzed by EDTA-1D-RP-n

21 from complex peptide mixtures of ovalbumin, alpha-casein, and beta-casein digests were also achieved

22 d was developed for allergens analysis using alpha-casein as the biomarker for cow's milk detection,

23 or demonstrated good selectivity towards the alpha-casein as the target analyte and adequate recoveri

24 This suggests that alpha-casein assists folding by the TBR mechanism.

25 e its higher content of proline, compared to alpha-casein, beta-casein did not always have a higher a

26 des from tryptic digest of standard protein (alpha-casein, beta-casein, and commercially available ca

27 amide I band of alpha-synuclein, phosvitin, alpha-casein, beta-casein, and the non-A beta component

28 h as the higher total protein, total casein, alpha-casein, beta-casein, kappa-casein and alpha-tocoph

29 alpha-Casein, beta-casein, osteopontin, and chordin-like

30 ed when carboxymethylated bovine albumin and alpha-casein, considered to mimic proteins with extended

31 Bovine alpha-casein (containing alpha(s1)- and alpha(s2)-casein

32 phosphopeptides in mid-femtomole amounts of alpha-casein digests per MALDI spot.

33 For alpha-casein, four sites of phosphorylation were identif

34 and the hydrophobicity profiles we show that alpha-casein has a pair of helices that have similar seq

35 sted from a complex mixture containing 7% of alpha-casein identified 21 out of 22 phosphorylation sit

36 bacterial culture was mixed with the BODIPY-alpha-casein in a buffer of an appropriate pH and the de

37 idase activities were stimulated strongly by alpha-casein in the case of Ms-Lon but weakly by alpha-c

38 a-casein in the case of Ms-Lon but weakly by alpha-casein in the cases of N-G91 and N-E226.

39 degradation of the Ms-Lon protein substrates alpha-casein in vitro and RcsA in vivo.

40 ptides identified in the acid hydrolysate of alpha casein increased by 45% and the number of peptides

41 BODIPY-alpha-casein is a new fluorescent protein substrate desi

42 Addition of alpha-casein partially substitutes for Mg(2+) in activat

43 The gold sensor chip was used to immobilise alpha-casein-polyclonal antibody using EDC/NHS coupling

44 entify residues that stabilize (destabilize) alpha-casein-protein complexes.

45 sequence information of a tryptic digest on alpha-casein s1.

46 Bovine serum albumin, lactoferrin, and alpha-casein (S1 and S2 forms, as was revealed by MALDI

47 3 triphosphopeptides were identified in the alpha-casein sample, while 19 mono-, 8 di-, 4 tri-, and

48 comparing this result with dephosphorylated alpha-casein, spectral variations in phosphate stretch b

49 Measured phosphopeptide fold-changes from alpha-casein spiked into wild-type zebrafish lysate back

50 rocyanidin A1 displayed a higher affinity to alpha-casein than the supposedly more flexible B-type di

51 EVSLNSGYY, barley; PGTAVFK, soybean; TTMPLW, alpha-casein; VHLPP, alpha-zein) and the six alanine sub

52 (ii) A sample of trypsin-digested alpha-casein was derivatized with [3H]CM-DTT, peptides w

53 se during the NH2-terminal aminoacylation of alpha-casein, whereas Val-tRNAVal-1 (UAC), Val-tRNAMetm

54 omparing the structures of the non-chaperone alpha-casein (which has no sequence similarity with the