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1 eration whey protein ingredients enriched in alpha-lactalbumin.
2 denaturation of the globular protein, human alpha-lactalbumin.
3 mplex of bovine Gal-T1-Mn(2+)-UDP-GalNAc-Glc-alpha-lactalbumin.
4 of a series of proline variants of [28-111] alpha-lactalbumin.
5 osecond dynamics of native and the denatured alpha-lactalbumin.
6 he complex of alphaB-crystallin and unfolded alpha-lactalbumin.
7 ne resonances of the molten globule state of alpha-lactalbumin.
8 by Dobson and Kim for the homologous protein alpha-lactalbumin.
9 ptide containing only residues 101 to 111 of alpha-lactalbumin.
10 nd to the reduced, carboxymethylated form of alpha-lactalbumin.
11 he permeability of endothelial monolayers to alpha-lactalbumin.
12 larly evident for 125I-alpha-globin and 125I-alpha-lactalbumin.
13 of the native main chain fold of apo bovine alpha-lactalbumin.
14 tion were mainly composed of lactoferrin and alpha-lactalbumin.
15 n the retention of infliximab, lysozyme, and alpha-lactalbumin.
16 peptides derived from beta-lactoglobulin and alpha-lactalbumin.
17 at are stabilized by the milk metalloprotein alpha-lactalbumin.
18 s approximately 1.3 times as high as that of alpha-Lactalbumin.
19 tates of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants
20 ion of four proteins, bovine S-carboxymethyl-alpha-lactalbumin (a disordered form of the protein with
22 e immunized SWXJ mice with recombinant mouse alpha-lactalbumin, a lactation-dependent, breast-specifi
23 egies to characterize sHSP interactions with alpha-lactalbumin, a model client whose aggregation path
26 to determine whether the disulfide bonds of alpha-lactalbumin account for the lack of cooperative fo
27 as decreased from pH 7 toward pH 2, at which alpha-lactalbumin adopts a molten globule state, a small
29 creasing degree of suppression of insulin or alpha-lactalbumin aggregation correlated with a decreasi
30 cheese whey (CW), beta-lactoglobulin (BLG), alpha-lactalbumin (ALA) and bovine serum albumin (BSA).
34 ting known bovine milk IgE-binding epitopes [alpha-lactalbumin (ALA), beta- and kappa-casein] and the
35 , namely cationic lysozyme (Lys) and anionic alpha-lactalbumin (aLac), both of which can be found in
40 heating cow milk at 80 degrees C for 60min, alpha-lactalbumin (alpha-la) and beta-lactoglobulin (bet
42 The reversible thermal denaturation of apo alpha-lactalbumin (alpha-LA) and lysozyme was measured i
43 camel milk at 80 degrees C for 60min, camel alpha-lactalbumin (alpha-la) and peptidoglycan recogniti
44 tion (HPH) and pH-shifting on the mixture of alpha-lactalbumin (alpha-LA) and tryptophan (Trp) was us
45 he free energy of unfolding (DeltaG(D-N)) of alpha-lactalbumin (alpha-LA) as a function of net charge
46 pectively without and with Ca(2+)) of bovine alpha-lactalbumin (alpha-La) at different temperatures,
47 fluorescence properties of three variants of alpha-lactalbumin (alpha-LA) containing a single tryptop
48 ast Flow gel column) was developed to purify alpha-lactalbumin (alpha-LA) from whey protein isolate.
55 The 15N-1H HSQC NMR spectrum of the human alpha-lactalbumin (alpha-LA) molten globule at pH 2 and
56 his variant has been used as a model for the alpha-lactalbumin (alpha-LA) molten globule in a number
57 to study the adsorption of Alexa 555 labeled alpha-lactalbumin (alpha-LA) on two chemically identical
58 LA(alpha), a two- disulfide variant of human alpha-lactalbumin (alpha-LA) that adopts a molten globul
59 ionation of beta-lactoglubulin (beta-lg) and alpha-lactalbumin (alpha-la) using conventional separati
60 ously identified calcium binding residues in alpha-lactalbumin (alpha-LA) was investigated by site-di
61 Results showed that increased contents of alpha-lactalbumin (alpha-La) were associated with increa
63 fatty acids (FAs), lipid peroxides (LP) and alpha-lactalbumin (alpha-La) were on a similar level as
65 side-chain packing in the molten globule of alpha-lactalbumin (alpha-LA), a highly fluctuating, non-
66 t whey proteins, bovine serum albumin (BSA), alpha-lactalbumin (alpha-LA), and two genetic variants o
68 y proteins, beta-Lactoglobulin (beta-Lg) and alpha-lactalbumin (alpha-La), was achieved after 4 h, at
71 reviously for the archetypal molten globule, alpha-lactalbumin (alpha-LA); this difference may be due
73 eins including beta-lactoglobulin (beta-Lg), alpha-lactalbumin (alpha-Lac), and bovine serum albumin
74 binding strength was reduced in the order of alpha-lactalbumin (alpha-Lact), whey protein isolate (WP
75 structures of complexes made of the proteins alpha-Lactalbumin (alphaLA) and myoglobin (Mb) with the
76 e) and in the presence of a thiol initiator, alpha-lactalbumin (alphaLA) denatures by shuffling its f
83 mmunoglobulin, lactoperoxidase, lactoferrin, alpha-lactalbumin and beta-lactoglobulin from sheep chee
90 the alpha-helical domain is observed in both alpha-lactalbumin and c-type lysozyme; however, the deta
91 ere dependent on the approach used to enrich alpha-lactalbumin and concentrations of other macromolec
92 rsistent expression of the milk protein gene alpha-lactalbumin and delayed expression of genes associ
93 guously identify the peak as a fragment from alpha-lactalbumin and eliminate a large number of spurio
95 BSA, the residues of aromatic cluster II in alpha-lactalbumin and into the calyx of beta-lactoglobul
96 C/15 s, 75 degrees C/15 min), IMF containing alpha-lactalbumin and lactoferrin preserved a higher pro
97 fference in kinetic folding pathways between alpha-lactalbumin and lysozyme can be explained by the d
99 r in preventing the amorphous aggregation of alpha-lactalbumin and the amyloid fibril formation of al
100 B-crystallin became entangled with unfolding alpha-lactalbumin and was a major portion of the resulti
101 RNA levels of endogenous MMTV as well as alpha-lactalbumin and whey acidic protein (WAP) were ele
105 and scrambled disulfide linkages of insulin, alpha-lactalbumin, and bovine serum albumin (BSA) as wel
106 ns in a mixture (e.g., beta-lactoglobulin B, alpha-lactalbumin, and carbonic anhydrase) by CMS in one
107 For gammaII-crystallin, myoglobin, barnase, alpha-lactalbumin, and cytochrome c the foldons and some
108 that of a single disulfide variant, [28-111] alpha-lactalbumin, and of a series of proline variants o
109 lies of c-type lysozyme and one subfamily of alpha-lactalbumin are defined from 78 sequences, and the
113 ed that the levels of beta-lactoglobulin and alpha-lactalbumin associated with the casein micelles in
114 with beta-casein recovery at 64 +/- 1 % and alpha-lactalbumin at 85 +/- 2 % after storage of 14 days
115 s reinforced the structural stability of the alpha-lactalbumin at high temperature and its resistance
116 he molten globule state from measurements on alpha-lactalbumin at pH 2.0 over the temperature range 2
117 he milk allergen component-specific (casein, alpha-lactalbumin, B-lactoglobulin) immunoglobulin (sIg
118 were discovered for chordin-like protein 2, alpha-lactalbumin, beta-1,4-galactosyl transferase, and
119 also a source of allergenic proteins such as alpha-lactalbumin, beta-lactoglobulin (BLG), casein, and
120 ower limits of detection for model proteins, alpha-lactalbumin, beta-lactoglobulin A, and beta-lactog
122 uccessful OIT outcome, as high IgE levels to alpha-lactalbumin, beta-lactoglobulin and casein are ass
123 The kinetics of heat-induced denaturation of alpha-lactalbumin, beta-lactoglobulin and lactoferrin we
124 peroxidase, bovine serum albumin) and major (alpha-lactalbumin, beta-lactoglobulin) whey proteins.
125 Humanising' the model formulas by increasing alpha-lactalbumin:beta-lactoglobulin enhanced heat stabi
128 protein-protein interactions with increasing alpha-lactalbumin:beta-lactoglobulin has important impli
129 ms (5.5% protein) were formulated to contain alpha-lactalbumin:beta-lactoglobulin ratios of 0.1, 0.5,
130 icated that increased heat stability in high alpha-lactalbumin:beta-lactoglobulin samples was due to
134 olding of the molten globule state of bovine alpha-lactalbumin (BLA) has been obtained using NMR spec
135 e Ca(2+)-free apo form of recombinant bovine alpha-lactalbumin (BLA) is sufficiently stabilised in it
136 s of 125I-labeled human alpha-globin, bovine alpha-lactalbumin, bovine serum albumin, or chicken lyso
137 w-A, consists of residues 72-100 from bovine alpha-lactalbumin, but with Cys 73, Cys 77, and Cys 91 r
138 values lower than the limit of detection and alpha-lactalbumin by approximately 34%, and was reduced
139 Thus, molten globule formation in human alpha-lactalbumin can be driven by the isolated alpha-su
140 main of ribosomal protein L9 (CTL9), FKBP12, alpha-lactalbumin, colicin E7 immunity protein 7 (IM7),
144 ts derived from the alpha-subdomain of human alpha-lactalbumin containing the A, B, D, and 3(10) heli
145 havior of the low-pH molten globule of human alpha-lactalbumin, containing all four disulfides, has b
146 whereas its complex with the substrates and alpha-lactalbumin, crystallizes in a conformation (2.3A
147 wn non-two-state folding proteins, including alpha-lactalbumin, cytochrome c, intestinal fatty acid b
148 similar to the molten globule state of human alpha-lactalbumin, demonstrates a marginal increase in t
149 ta shows that the heat capacity increment of alpha-lactalbumin denaturation highly correlates with th
151 In good agreement, the 3D structure of camel alpha-lactalbumin determined by X-ray crystallography, d
152 ed dissociation of an unassigned peak in the alpha-lactalbumin digest provided sufficient data to una
153 tion of R120G alphaB-crystallin to unfolding alpha-lactalbumin enhanced the kinetics and extent of it
154 andard formula, protein-reduced formula with alpha-lactalbumin-enriched whey, or protein-reduced form
155 rying conditions than beta-lactoglobulin and alpha-lactalbumin, especially at longer drying times.
157 tiary structure, whereas the intermediate of alpha-lactalbumin exhibits the characteristics of a molt
161 edure was used to study the refolding of apo alpha-lactalbumin following dilution from guanidinium ch
164 s a result, the denaturational transition of alpha-lactalbumin from the native to a highly ordered co
168 dynamics of the molten globule (MG) state of alpha-lactalbumin have been characterized using (15)N tr
170 ted versus flat) of fibrils of lysozyme, apo-alpha-lactalbumin, HET-s (218-289) prion, and a short po
171 In agreement with previous studies on human alpha-lactalbumin (HLA) the unfolding process for BLA ha
172 an form various complexes with native bovine alpha-lactalbumin (holo-ALA) and decalcified-ALA (apo-AL
173 s of both cytochrome c and disulfide-reduced alpha-lactalbumin homodimers dissociate by a symmetrical
175 iting E3alpha-catalyzed conjugation to human alpha-lactalbumin, HsUbc2b-ubiquitin thiolester exhibits
176 es of non-native states of the protein human alpha-lactalbumin (human alpha-LA) with a detailed atomi
177 ar, CI2, spectrin R16 domain, Arc repressor, alpha-lactalbumin, IM7, IM9, and spectrin R17 domain.
178 fertility and birth numbers, pups nursed by alpha-lactalbumin-immunized mice showed significantly di
180 oreover, the partially unfolded structure of alpha-lactalbumin in the nanoprobe helps with the format
182 a protein mixture consisting of transferrin, alpha-lactalbumin, insulin, and alpha-2-macroglobulin.
183 sults revealed a reduction in the casein and alpha-lactalbumin intensity bands after SD or GD treatme
186 esponding to residues 101-111 of the protein alpha-lactalbumin is remarkably structured in isolation
188 ds (human carbonic anhydrase I, enolase, and alpha-lactalbumin) is achieved at 50- to 100-fold excess
190 ression of a fusion protein comprising human alpha lactalbumin joined by an enterokinase cleavable li
191 gated using six proline variants of [28-111] alpha-lactalbumin, L11P, L12P, M30P, I95P, K108P and Q11
194 se (beta4Gal-T1) and a regulatory component, alpha-lactalbumin (LA), a mammary gland-specific protein
199 le describes some of these proteins, such as alpha-lactalbumin, lactoferrin, osteopontin, and milk fa
200 transcripts, encoding beta-casein (CSN2) and alpha-lactalbumin (LALBA), make up 45% of the total pool
201 rast to the isolated alpha-helical domain of alpha-lactalbumin, Lyso-alpha with two native disulfide
204 extraordinary manner in which HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells) kills a wi
205 acid/alpha-lactalbumin complex HAMLET (human alpha-lactalbumin made lethal to tumors) is cytotoxic to
206 unable to fold denatured substrates such as alpha-lactalbumin, malate dehydrogenase (MDH), and the b
210 n E3alpha-catalyzed conjugation of the human alpha-lactalbumin N-end rule substrate shows Ubc2bS120D
213 n 125I-lysozyme turnover, and decreased 125I-alpha-lactalbumin or 125I-albumin degradation by approxi
214 vents: The ATP-dependent degradation of 125I-alpha-lactalbumin or 125I-albumin is probably mediated a
216 tion had a larger increase in IgG4 levels to alpha-lactalbumin (P = 0.034), beta-lactoglobulin (P = 0
217 ecific IgE levels towards the milk allergens alpha-lactalbumin (P = 0.048), beta-lactoglobulin (P = 0
220 , did not fibrillate, although Zn(2+)-loaded alpha-lactalbumin precipitated out of solution as amorph
221 whey protein concentrate systems enriched in alpha-lactalbumin, produced using membrane filtration (L
222 of the whey proteins, beta-lactoglobulin and alpha-lactalbumin, promoted colour change from blue to r
223 ddition, the immobilized derivate hydrolyzed alpha-lactalbumin protein with a higher affinity than be
224 iate parameters enabled the reaction between alpha-lactalbumin proteins and cross-linkers using a non
225 om human milk but did affect lactoferrin and alpha-lactalbumin proteolysis and emulsion disintegratio
227 bumin to 82 +/- 1 %, with the beta-casein-to-alpha-lactalbumin recovery ratio reaching 97 +/- 8 % aft
228 ow or no peptides for beta-Lactoglobulin and alpha-Lactalbumin, respectively, suggest these proteins
229 both CKbeta4GT-I and CKbeta4GT-II encode an alpha-lactalbumin-responsive, UDP-galactose:N-acetylgluc
230 reased levels of MMTV, beta-casein, WAP, and alpha-lactalbumin RNA in virgin mammary glands compared
233 A mixture of bovine carbonic anhydrase, alpha-lactalbumin, soybean trypsin inhibitor, and ovalbu
234 e Camelidae family are the only of described alpha-lactalbumins that carry two AsnGly sequences.
235 -casein recovery increased to 80 +/- 6 % and alpha-lactalbumin to 82 +/- 1 %, with the beta-casein-to
236 enthalpy and entropy of the denaturation of alpha-lactalbumin to compact denatured state are always
239 n peptide release from human lactoferrin and alpha-lactalbumin was observed when HM was supplemented
240 Results showed that the heat-denaturation of alpha-lactalbumin was reduced when beta-lactoglobulin wa
243 ration, the percentage of positive cells for alpha-lactalbumin was significantly higher when compared
244 on, the most active chaperone of insulin and alpha-lactalbumin was the Hsp27 (elongated) dimer, the s
246 , BSA, beta-lactoglobulin, alpha-casein, and alpha-lactalbumin, was achieved, using either the ultras
248 epithelial marker CK14, and lactocyte marker alpha-lactalbumin were amongst the genes most highly exp
252 emulsions with the highest concentration of alpha-lactalbumin were most stable to oxidation during s
253 simulations of GMP, de-glycosylated GMP, and alpha-lactalbumin were performed and confirmed substanti
254 es binding sites for the oligosaccharide and alpha-lactalbumin, when compared to the ligand-free stru
255 The calcium-depleted form of the protein alpha-lactalbumin, which displays a cluster of acidic am
257 nd gave very few spurious masses, and bovine alpha-lactalbumin, which under the conditions used, gave
258 ty with norbixin than beta-lactoglobulin and alpha-lactalbumin, while kappa-casein bound with norbixi
259 red by the aggregation of reduced insulin or alpha-lactalbumin, with Hsp27 self-association as monito