ライフサイエンスコーパス: lactalbumin

1 n the degradation of a model substrate (125I-lactalbumin).

2 uration of the globular protein, human alpha-lactalbumin.

3 n whey protein ingredients enriched in alpha-lactalbumin.

4 rom either high-isoflavone soy or casein and lactalbumin.

5 of bovine Gal-T1-Mn(2+)-UDP-GalNAc-Glc-alpha-lactalbumin.

6 series of proline variants of [28-111] alpha-lactalbumin.

7 d dynamics of native and the denatured alpha-lactalbumin.

8 plex of alphaB-crystallin and unfolded alpha-lactalbumin.

9 onances of the molten globule state of alpha-lactalbumin.

10 son and Kim for the homologous protein alpha-lactalbumin.

11 containing only residues 101 to 111 of alpha-lactalbumin.

12 the reduced, carboxymethylated form of alpha-lactalbumin.

13 meability of endothelial monolayers to alpha-lactalbumin.

14 evident for 125I-alpha-globin and 125I-alpha-lactalbumin.

15 e native main chain fold of apo bovine alpha-lactalbumin.

16 on were mainly composed of lactoferrin and a-lactalbumin.

17 ere mainly composed of lactoferrin and alpha-lactalbumin.

18 tment induced the insoluble aggregation of a-lactalbumin.

19 retention of infliximab, lysozyme, and alpha-lactalbumin.

20 es derived from beta-lactoglobulin and alpha-lactalbumin.

21 stabilized by the milk metalloprotein alpha-lactalbumin.

22 oximately 1.3 times as high as that of alpha-Lactalbumin.

23 of a single-disulfide variant of human alpha-lactalbumin ([28-111] alpha-LA) and of two mutants, each

24 four proteins, bovine S-carboxymethyl-alpha-lactalbumin (a disordered form of the protein with reduc

25 a-lactalbumin (a-la) and B-lg appear red while GMP stains

26 a-lactalbumin (a-la) and beta-lg appear red while GMP stai

27 ctively without and with Ca(2+)) of bovine a-lactalbumin (a-La) at different temperatures, and to cor

28 atty acids (FAs), lipid peroxides (LP) and a-lactalbumin (a-La) were on a similar level as in raw mil

29 whey proteins, B-Lactoglobulin (B-Lg) and a-lactalbumin (a-La), was achieved after 4 h, at E/S ratio

30 d that Protease M preferentially hydrolyzeda-lactalbumin (a-la), while trypsin targeted B-lactoglobul

31 S-(Carboxymethyl)-alpha-lactalbumin, a disordered form of the protein with three

32 nized SWXJ mice with recombinant mouse alpha-lactalbumin, a lactation-dependent, breast-specific diff

33 to characterize sHSP interactions with alpha-lactalbumin, a model client whose aggregation pathway is

34 Bovine alpha-lactalbumin, a small acidic Ca(2+)-binding milk protein,

35 alpha-Lactalbumin, a small calcium-binding protein, forms an e

36 termine whether the disulfide bonds of alpha-lactalbumin account for the lack of cooperative folding

37 reased from pH 7 toward pH 2, at which alpha-lactalbumin adopts a molten globule state, a small but i

38 tually even inhibited the formation of alpha-lactalbumin aggregates.

39 ng degree of suppression of insulin or alpha-lactalbumin aggregation correlated with a decreasing Hsp

40 e whey (CW), beta-lactoglobulin (BLG), alpha-lactalbumin (ALA) and bovine serum albumin (BSA).

41 erous cell lines and is assembled from alpha-lactalbumin (ALA) and free oleic acid (OA).

42 HAMLET is a complex of human alpha-lactalbumin (ALA) and oleic acid and kills several Gram-

43 1) and type-3 (without calcium, ALA-3) alpha-lactalbumin (ALA) were examined.

44 nown bovine milk IgE-binding epitopes [alpha-lactalbumin (ALA), beta- and kappa-casein] and the corre

45 ly cationic lysozyme (Lys) and anionic alpha-lactalbumin (aLac), both of which can be found in the ci

46 By using alpha-lactalbumin, alcohol dehydrogenase, and insulin as targe

47 tablish a nanozyme-based ELISA towards alpha-lactalbumin (allergenic protein).

48 The pathway of oxidative folding of alpha-lactalbumin (alpha LA) (four disulfide bonds) has been c

49 alpha-Lactalbumin (alpha LA) forms a well-populated equilibriu

50 ng cow milk at 80 degrees C for 60min, alpha-lactalbumin (alpha-la) and beta-lactoglobulin (beta-lg)

51 Bovine alpha-lactalbumin (alpha-La) and kappa-casein (CN) displayed t

52 reversible thermal denaturation of apo alpha-lactalbumin (alpha-LA) and lysozyme was measured in the

53 milk at 80 degrees C for 60min, camel alpha-lactalbumin (alpha-la) and peptidoglycan recognition pro

54 HPH) and pH-shifting on the mixture of alpha-lactalbumin (alpha-LA) and tryptophan (Trp) was used to

55 e energy of unfolding (DeltaG(D-N)) of alpha-lactalbumin (alpha-LA) as a function of net charge.

56 ely without and with Ca(2+)) of bovine alpha-lactalbumin (alpha-La) at different temperatures, and to

57 scence properties of three variants of alpha-lactalbumin (alpha-LA) containing a single tryptophan re

58 ow gel column) was developed to purify alpha-lactalbumin (alpha-LA) from whey protein isolate.

59 The structure of denatured alpha-lactalbumin (alpha-LA) has been characterized using the

60 The molten globule state of alpha-lactalbumin (alpha-LA) has been considered a prototype o

61 Bovine alpha-lactalbumin (alpha-LA) has been shown by intrinsic prote

62 Recently, the molten globule of alpha-lactalbumin (alpha-LA) has been shown to adopt a native-

63 alpha-Lactalbumin (alpha-LA) is a two-domain calcium-binding p

64 Alpha-lactalbumin (alpha-LA) is one of the whey proteins in co

65 15N-1H HSQC NMR spectrum of the human alpha-lactalbumin (alpha-LA) molten globule at pH 2 and 20 deg

66 riant has been used as a model for the alpha-lactalbumin (alpha-LA) molten globule in a number of stu

67 dy the adsorption of Alexa 555 labeled alpha-lactalbumin (alpha-LA) on two chemically identical but m

68 ha), a two- disulfide variant of human alpha-lactalbumin (alpha-LA) that adopts a molten globule conf

69 on of beta-lactoglubulin (beta-lg) and alpha-lactalbumin (alpha-la) using conventional separation tec

70 identified calcium binding residues in alpha-lactalbumin (alpha-LA) was investigated by site-directed

71 ults showed that increased contents of alpha-lactalbumin (alpha-La) were associated with increased se

72 ed whey protein isolate (WPI) and pure alpha-lactalbumin (alpha-La) were investigated.

73 acids (FAs), lipid peroxides (LP) and alpha-lactalbumin (alpha-La) were on a similar level as in raw

74 ection of food allergic protein (i.e., alpha-lactalbumin (alpha-LA)).

75 chain packing in the molten globule of alpha-lactalbumin (alpha-LA), a highly fluctuating, non-cooper

76 proteins, bovine serum albumin (BSA), alpha-lactalbumin (alpha-LA), and two genetic variants of beta

77 For human alpha-lactalbumin (alpha-LA), the equilibrium molten globule i

78 eins, beta-Lactoglobulin (beta-Lg) and alpha-lactalbumin (alpha-La), was achieved after 4 h, at E/S r

79 s to a mammary gland-specific protein, alpha-lactalbumin (alpha-LA).

80 el of beta-lactoglobulin (beta-LG) and alpha-lactalbumin (alpha-LA).

81 sly for the archetypal molten globule, alpha-lactalbumin (alpha-LA); this difference may be due to a

82 Electrostatic interactions between alpha-lactalbumin (alpha-lac) and carboxymethyldextran (CMD) i

83 ncluding beta-lactoglobulin (beta-Lg), alpha-lactalbumin (alpha-Lac), and bovine serum albumin (BSA)

84 g strength was reduced in the order of alpha-lactalbumin (alpha-Lact), whey protein isolate (WPI), an

85 ures of complexes made of the proteins alpha-Lactalbumin (alphaLA) and myoglobin (Mb) with the biosur

86 in the presence of a thiol initiator, alpha-lactalbumin (alphaLA) denatures by shuffling its four na

87 Four proteins, BSA, alpha-lactalbumin (alphaLA), lysozyme, and beta-lactoglobulin

88 Alpha-lactalbumin (alphaLA)-IIIA is a major kinetic intermedia

89 olding and oxidative folding of bovine alpha-lactalbumin (alphaLA).

90 is a partially folded intermediate of alpha-lactalbumin (alphaLA).

91 s of the molten globule state of human alpha-lactalbumin (alphaLA).

92 a-globin to approximately 85% for 125I-alpha-lactalbumin and 125I-albumin.

93 lobulin, lactoperoxidase, lactoferrin, alpha-lactalbumin and beta-lactoglobulin from sheep cheese swe

94 the bioactivities of proteins, such as alpha-lactalbumin and beta-lactoglobulin in vitro.

95 Immune-reactive alpha-lactalbumin and beta-lactoglobulin were found in the two

96 immunocytochemistry for milk proteins: alpha-lactalbumin and beta-lactoglobulin.

97 ll improvement of pepsinolysis of both alpha-lactalbumin and beta-lactoglobulin.

98 rotein isolates with varying ratios of alpha-lactalbumin and beta-lactoglobulin.

99 Proteins in the alpha-lactalbumin and c-type lysozyme family have been studied

100 pha-helical domain is observed in both alpha-lactalbumin and c-type lysozyme; however, the details of

101 pendent on the approach used to enrich alpha-lactalbumin and concentrations of other macromolecules (

102 nt expression of the milk protein gene alpha-lactalbumin and delayed expression of genes associated w

103 y identify the peak as a fragment from alpha-lactalbumin and eliminate a large number of spurious pro

104 sts of residues 20 through 36 of human alpha-lactalbumin and includes the entire B-helix.

105 the residues of aromatic cluster II in alpha-lactalbumin and into the calyx of beta-lactoglobulin res

106 Interestingly, lactalbumin and lactoferrin decreased hepatic lipidosis

107 Lactalbumin and lactoferrin decreased plasma leptin and

108 Dietary lactalbumin and lactoferrin improved energy balance and

109 Whey, lactalbumin and lactoferrin improved glucose clearance p

110 , 75 degrees C/15 min), IMF containing alpha-lactalbumin and lactoferrin preserved a higher proportio

111 tein diets containing whey, or its fractions lactalbumin and lactoferrin, on energy balance and metab

112 ce in kinetic folding pathways between alpha-lactalbumin and lysozyme can be explained by the differe

113 oricidal complex of partially unfolded alpha-lactalbumin and oleic acid (OA).

114 reventing the amorphous aggregation of alpha-lactalbumin and the amyloid fibril formation of alpha-sy

115 tallin became entangled with unfolding alpha-lactalbumin and was a major portion of the resulting ins

116 A levels of endogenous MMTV as well as alpha-lactalbumin and whey acidic protein (WAP) were elevated.

117 The alpha-lactalbumins and c-type lysozymes have virtually identic

118 r proteins (bovine serum albumin, ovalbumin, lactalbumin) and four narrow fractions of Ficoll, were s

119 lactoglobulin A, beta-lactoglobulin B, alpha-lactalbumin, and albumin).

120 e, pyruvate kinase, albumin, lysozyme, alpha-lactalbumin, and beta-lactoglobulin.

121 rambled disulfide linkages of insulin, alpha-lactalbumin, and bovine serum albumin (BSA) as well as t

122 d scrambled disulfide linkages of insulin, a-lactalbumin, and bovine serum albumin (BSA) as well as t

123 a mixture (e.g., beta-lactoglobulin B, alpha-lactalbumin, and carbonic anhydrase) by CMS in one run,

124 ammaII-crystallin, myoglobin, barnase, alpha-lactalbumin, and cytochrome c the foldons and some nonco

125 f a single disulfide variant, [28-111] alpha-lactalbumin, and of a series of proline variants of [28-

126 f c-type lysozyme and one subfamily of alpha-lactalbumin are defined from 78 sequences, and their fol

127 Casein, beta-lactoglobulin and alpha-lactalbumin are major milk protein allergens.

128 Casein, B-lactoglobulin and a-lactalbumin are major milk protein allergens.

129 Using insulin and alpha-lactalbumin as model target proteins, we also show that

130 We selected alpha-lactalbumin as our target vaccine autoantigen because it

131 ne the effects of two diets, one with casein-lactalbumin as the main protein source and the other wit

132 re fed diets that contained either 1) casein-lactalbumin as the source of protein (casein), 2) soy pr

133 t the levels of beta-lactoglobulin and alpha-lactalbumin associated with the casein micelles increase

134 beta-casein recovery at 64 +/- 1 % and alpha-lactalbumin at 85 +/- 2 % after storage of 14 days.

135 forced the structural stability of the alpha-lactalbumin at high temperature and its resistance towar

136 ten globule state from measurements on alpha-lactalbumin at pH 2.0 over the temperature range 2 to 45

137 k allergen component-specific (casein, alpha-lactalbumin, B-lactoglobulin) immunoglobulin (sIg [sIgE,

138 roxidase, bovine serum albumin) and major (a-lactalbumin, B-lactoglobulin) whey proteins.

139 discovered for chordin-like protein 2, alpha-lactalbumin, beta-1,4-galactosyl transferase, and poly-I

140 source of allergenic proteins such as alpha-lactalbumin, beta-lactoglobulin (BLG), casein, and immun

141 imits of detection for model proteins, alpha-lactalbumin, beta-lactoglobulin A, and beta-lactoglobuli

142 The aggregation of alpha-lactalbumin, beta-lactoglobulin and beta-casein after he

143 ful OIT outcome, as high IgE levels to alpha-lactalbumin, beta-lactoglobulin and casein are associate

144 netics of heat-induced denaturation of alpha-lactalbumin, beta-lactoglobulin and lactoferrin were inv

145 dase, bovine serum albumin) and major (alpha-lactalbumin, beta-lactoglobulin) whey proteins.

146 sing' the model formulas by increasing alpha-lactalbumin:beta-lactoglobulin enhanced heat stability a

147 In low alpha-lactalbumin:beta-lactoglobulin formulas, protein-protein

148 between proteins were minimal in high alpha-lactalbumin:beta-lactoglobulin formulas.

149 n-protein interactions with increasing alpha-lactalbumin:beta-lactoglobulin has important implication

150 5% protein) were formulated to contain alpha-lactalbumin:beta-lactoglobulin ratios of 0.1, 0.5, 1.3,

151 that increased heat stability in high alpha-lactalbumin:beta-lactoglobulin samples was due to decrea

152 nts indicate that reduced, carboxymethylated lactalbumin binds Hip with a Kd of 5 microM.

153 The internal dynamics of bovine alpha-lactalbumin (BLA) and its molten globules (MBLA) have be

154 Prolonged heating of holo bovine alpha-lactalbumin (BLA) at 80 degrees C in pH 7 phosphate buff

155 The refolding of bovine alpha-lactalbumin (BLA) from its chemically denatured state in

156 of the molten globule state of bovine alpha-lactalbumin (BLA) has been obtained using NMR spectrosco

157 +)-free apo form of recombinant bovine alpha-lactalbumin (BLA) is sufficiently stabilised in its nati

158 25I-labeled human alpha-globin, bovine alpha-lactalbumin, bovine serum albumin, or chicken lysozyme w

159 onsists of residues 72-100 from bovine alpha-lactalbumin, but with Cys 73, Cys 77, and Cys 91 replace

160 lower than the limit of detection and alpha-lactalbumin by approximately 34%, and was reduced furthe

161 hus, molten globule formation in human alpha-lactalbumin can be driven by the isolated alpha-subdomai

162 s as substrates (insulin-like growth factor, lactalbumin, casein, and alkaline phosphatase, whose len

163 f ribosomal protein L9 (CTL9), FKBP12, alpha-lactalbumin, colicin E7 immunity protein 7 (IM7), colici

164 The oleic acid/alpha-lactalbumin complex HAMLET (human alpha-lactalbumin made

165 nd P = 0.044), and a positive association of lactalbumin concentration with motor skills (P = 0.038).

166 alpha-Lactalbumin consists of two subdomains, and the alpha-su

167 ss structured and less stable than the alpha-lactalbumin construct.

168 ived from the alpha-subdomain of human alpha-lactalbumin containing the A, B, D, and 3(10) helices ar

169 of the low-pH molten globule of human alpha-lactalbumin, containing all four disulfides, has been ex

170 as its complex with the substrates and alpha-lactalbumin, crystallizes in a conformation (2.3A resolu

171 -two-state folding proteins, including alpha-lactalbumin, cytochrome c, intestinal fatty acid binding

172 Lactalbumin decreased weight and fat gain.

173 r to the molten globule state of human alpha-lactalbumin, demonstrates a marginal increase in the amo

174 ws that the heat capacity increment of alpha-lactalbumin denaturation highly correlates with the degr

175 Relatively potent alpha-lactalbumin-derived DPP-IV inhibitory peptides (LAHKPL a

176 d agreement, the 3D structure of camel alpha-lactalbumin determined by X-ray crystallography, display

177 sociation of an unassigned peak in the alpha-lactalbumin digest provided sufficient data to unambiguo

178 f R120G alphaB-crystallin to unfolding alpha-lactalbumin enhanced the kinetics and extent of its aggr

179 formula, protein-reduced formula with alpha-lactalbumin-enriched whey, or protein-reduced formula wi

180 conditions than beta-lactoglobulin and alpha-lactalbumin, especially at longer drying times.

181 rom one another; the stronger one, apo-alpha-lactalbumin, exhibited a Kd of 35 microM.

182 structure, whereas the intermediate of alpha-lactalbumin exhibits the characteristics of a molten glo

183 ic for non-native domains since native alpha-lactalbumin fails to interact with Hip.

184 al features characteristic of a native alpha-lactalbumin fold.

185 The calcium binding protein alpha-lactalbumin folds via a molten globule intermediate.

186 was used to study the refolding of apo alpha-lactalbumin following dilution from guanidinium chloride

187 isplayed a strong immunoreactivity for alpha-lactalbumin for 2-96 h.

188 All alpha-lactalbumins form a well populated molten globule state,

189 sult, the denaturational transition of alpha-lactalbumin from the native to a highly ordered compact

190 Two different alpha-lactalbumin genetic constructs are studied: [28-111], wh

191 Although immunization with alpha-lactalbumin had no effect on fertility and birth numbers

192 s in stabilizing the molten globule of alpha-lactalbumin has been prepared.

193 cs of the molten globule (MG) state of alpha-lactalbumin have been characterized using (15)N transver

194 Structures of human alpha-lactalbumin have been generated with significantly diffe

195 rsus flat) of fibrils of lysozyme, apo-alpha-lactalbumin, HET-s (218-289) prion, and a short polypept

196 reement with previous studies on human alpha-lactalbumin (HLA) the unfolding process for BLA has been

197 m various complexes with native bovine alpha-lactalbumin (holo-ALA) and decalcified-ALA (apo-ALA).

198 oth cytochrome c and disulfide-reduced alpha-lactalbumin homodimers dissociate by a symmetrical charg

199 Similar results are observed for alpha-lactalbumin homodimers.

200 E3alpha-catalyzed conjugation to human alpha-lactalbumin, HsUbc2b-ubiquitin thiolester exhibits a K(i

201 non-native states of the protein human alpha-lactalbumin (human alpha-LA) with a detailed atomistic m

202 2, spectrin R16 domain, Arc repressor, alpha-lactalbumin, IM7, IM9, and spectrin R17 domain.

203 lity and birth numbers, pups nursed by alpha-lactalbumin-immunized mice showed significantly disrupte

204 The change in structure of bovine alpha-lactalbumin in environments of decreasing pH from pH 7 t

205 r, the partially unfolded structure of alpha-lactalbumin in the nanoprobe helps with the formation of

206 rin decreased plasma leptin and insulin, and lactalbumin increased peptide YY.

207 -crystallin in preventing the aggregation of lactalbumin induced by dithiothreitol.

208 The effect of deamidation on camel alpha-lactalbumin instability was investigated.

209 ein mixture consisting of transferrin, alpha-lactalbumin, insulin, and alpha-2-macroglobulin.

210 revealed a reduction in the casein and alpha-lactalbumin intensity bands after SD or GD treatments; h

211 lts revealed a reduction in the casein and a-lactalbumin intensity bands after SD or GD treatments; h

212 Because alpha-lactalbumin is conditionally expressed only during lacta

213 nonnative structure for the folding of alpha-lactalbumin is discussed.

214 ing to residues 101-111 of the protein alpha-lactalbumin is remarkably structured in isolation in aqu

215 Camelid alpha-lactalbumin is the only known protein that can undergo n

216 man carbonic anhydrase I, enolase, and alpha-lactalbumin) is achieved at 50- to 100-fold excess of th

217 polymeric immunoglobulin receptor, and alpha-lactalbumin, is pH-dependent.

218 n of a fusion protein comprising human alpha lactalbumin joined by an enterokinase cleavable linker t

219 using six proline variants of [28-111] alpha-lactalbumin, L11P, L12P, M30P, I95P, K108P and Q117P.

220 In addition, alpha-lactalbumin (LA) enhances this Glc-T activity more than

221 Under reducing conditions where alpha-lactalbumin (LA) unfolds and aggregates, XaHspA 36mers f

222 ta4Gal-T1) and a regulatory component, alpha-lactalbumin (LA), a mammary gland-specific protein.

223 Aromatic cluster 1 of alpha-lactalbumin (LA), a substructure adjacent to the cleft,

224 ubstrates and to the modifier protein, alpha-lactalbumin (LA), by over 99%.

225 In the presence of alpha-lactalbumin (LA), it transfers Gal to Glc, which is its

226 In the presence of alpha-lactalbumin (LA), the Gal acceptor specificity is altere

227 1 individual HMOs, and 6 bioactive proteins (lactalbumin, lactoferrin, lysozyme, antitrypsin, IgA, an

228 ndomized to isocaloric diets: Control, Whey, Lactalbumin, Lactoferrin, or pair-fed to lactoferrin.

229 cribes some of these proteins, such as alpha-lactalbumin, lactoferrin, osteopontin, and milk fat glob

230 ripts, encoding beta-casein (CSN2) and alpha-lactalbumin (LALBA), make up 45% of the total pool of mR

231 o the isolated alpha-helical domain of alpha-lactalbumin, Lyso-alpha with two native disulfide bonds

232 of hen lysozyme and a set of chimeric alpha-lactalbumin--lysozyme constructs.

233 HAMLET (human alpha-lactalbumin made lethal to tumor cells) is a tumoricidal

234 ordinary manner in which HAMLET (Human Alpha-lactalbumin Made LEthal to Tumor cells) kills a wide ran

235 lpha-lactalbumin complex HAMLET (human alpha-lactalbumin made lethal to tumors) is cytotoxic to vario

236 e to fold denatured substrates such as alpha-lactalbumin, malate dehydrogenase (MDH), and the beta-su

237 in determining the overall fold of the alpha-lactalbumin molten globule.

238 However, in the case of alpha-lactalbumin more mass values were needed, and low mass e

239 y acidic protein mRNA was reduced, and alpha-lactalbumin mRNA was undetectable.

240 pha-catalyzed conjugation of the human alpha-lactalbumin N-end rule substrate shows Ubc2bS120D is 20-

241 The alpha-lactalbumins of members of the Camelidae family are the

242 oferrin (P < 0.01) and reduced that of alpha-lactalbumin (only at 90 min) (P < 0.05).

243 -lysozyme turnover, and decreased 125I-alpha-lactalbumin or 125I-albumin degradation by approximately

244 The ATP-dependent degradation of 125I-alpha-lactalbumin or 125I-albumin is probably mediated almost

245 in an 18-h ELISpot assay with casein, alpha-lactalbumin, or beta-lactoglobulin.

246 ad a larger increase in IgG4 levels to alpha-lactalbumin (P = 0.034), beta-lactoglobulin (P = 0.010),

247 IgE levels towards the milk allergens alpha-lactalbumin (P = 0.048), beta-lactoglobulin (P = 0.006)

248 ss structured and less stable than the alpha-lactalbumin peptide.

249 tructured than the corresponding human alpha-lactalbumin peptide.

250 ceiving soy diet premenopausally then casein/lactalbumin post-ovariectomy had higher relative hippoca

251 not fibrillate, although Zn(2+)-loaded alpha-lactalbumin precipitated out of solution as amorphous ag

252 Whey and lactalbumin produced transient hypophagia, whereas lacto

253 rotein concentrate systems enriched in alpha-lactalbumin, produced using membrane filtration (LAC-M),

254 whey proteins, beta-lactoglobulin and alpha-lactalbumin, promoted colour change from blue to red for

255 n, the immobilized derivate hydrolyzed alpha-lactalbumin protein with a higher affinity than beta-lac

256 arameters enabled the reaction between alpha-lactalbumin proteins and cross-linkers using a non-denat

257 an milk but did affect lactoferrin and alpha-lactalbumin proteolysis and emulsion disintegration.

258 We found that immunoreactivity against alpha-lactalbumin provides substantial protection and therapy

259 to 82 +/- 1 %, with the beta-casein-to-alpha-lactalbumin recovery ratio reaching 97 +/- 8 % after sto

260 f MCF7 cells with TDF led to production of a lactalbumin-related protein.

261 no peptides for beta-Lactoglobulin and alpha-Lactalbumin, respectively, suggest these proteins were h

262 CKbeta4GT-I and CKbeta4GT-II encode an alpha-lactalbumin-responsive, UDP-galactose:N-acetylglucosamin

263 levels of MMTV, beta-casein, WAP, and alpha-lactalbumin RNA in virgin mammary glands compared to tho

264 ELISA of casein and alpha-lactalbumin showed a decrease in antigenicity post plasm

265 ELISA of casein and a-lactalbumin showed a decrease in antigenicity post plasm

266 Mice immunized with alpha-lactalbumin showed extensive T-cell-mediated inflammatio

267 mixture of bovine carbonic anhydrase, alpha-lactalbumin, soybean trypsin inhibitor, and ovalbumin wa

268 lidae family are the only of described alpha-lactalbumins that carry two AsnGly sequences.

269 n recovery increased to 80 +/- 6 % and alpha-lactalbumin to 82 +/- 1 %, with the beta-casein-to-alpha

270 lpy and entropy of the denaturation of alpha-lactalbumin to compact denatured state are always greate

271 Thus, alpha-lactalbumin vaccination may provide safe and effective p

272 alpha-Lactalbumin was judiciously chosen as a spiked control t

273 a-Lactalbumin was judiciously chosen as a spiked control t

274 ide release from human lactoferrin and alpha-lactalbumin was observed when HM was supplemented with d

275 s showed that the heat-denaturation of alpha-lactalbumin was reduced when beta-lactoglobulin was abse

276 The alpha-Lactalbumin was relatively heat stable after drying and

277 alpha-Lactalbumin was selected as a model protein for the stud

278 , the percentage of positive cells for alpha-lactalbumin was significantly higher when compared with

279 e most active chaperone of insulin and alpha-lactalbumin was the Hsp27 (elongated) dimer, the smalles

280 In the raw milk, intact alpha-lactalbumin was visible on SDS - PAGE until the end of t

281 beta-lactoglobulin, alpha-casein, and alpha-lactalbumin, was achieved, using either the ultrasonic-b

282 A specific substrate of this pathway, alpha-lactalbumin, was ubiquitinated faster in the diabetic ex

283 lial marker CK14, and lactocyte marker alpha-lactalbumin were amongst the genes most highly expressed

284 The trypsin-digested spots of alpha-lactalbumin were analysed by MALDI-TOF mass spectrometry

285 Casein, B-lactoglobulin and a-lactalbumin were analyzed before and after plasma treatm

286 Casein, beta-lactoglobulin and alpha-lactalbumin were analyzed before and after plasma treatm

287 rees C, whereas 218+/-43 mg/L residual alpha-lactalbumin were found at 130 degrees C.

288 ions with the highest concentration of alpha-lactalbumin were most stable to oxidation during storage

289 tions of GMP, de-glycosylated GMP, and alpha-lactalbumin were performed and confirmed substantial dif

290 ding sites for the oligosaccharide and alpha-lactalbumin, when compared to the ligand-free structure.

291 e calcium-depleted form of the protein alpha-lactalbumin, which displays a cluster of acidic amino ac

292 The denatured states of alpha-lactalbumin, which have features of a molten globule sta

293 e very few spurious masses, and bovine alpha-lactalbumin, which under the conditions used, gave many

294 h norbixin than beta-lactoglobulin and alpha-lactalbumin, while kappa-casein bound with norbixin bett

295 the aggregation of reduced insulin or alpha-lactalbumin, with Hsp27 self-association as monitored by

296 dients, whey protein concentrate (WPC), whey lactalbumin (WLAC) and skim milk powder (SMP) on oat sta