PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23007873-7 2013 For this, we probe the structural stability of the calcium binding protein alpha-lactalbumin as a showcase, both in the "ground state" and after perturbing the system by changing the network topology. Calcium 51-58 lactalbumin alpha Homo sapiens 75-92 21524506-1 2011 alpha-Lactalbumin is a ubiquitous calcium-binding milk protein with a well-characterized function in regulating the synthesis of lactose. Calcium 34-41 lactalbumin alpha Homo sapiens 0-17 22417479-4 2011 Calcium significantly improved the thermal stability of alpha-lactalbumin and slowed down the formation of protein aggregates. Calcium 0-7 lactalbumin alpha Homo sapiens 56-73 22417479-8 2011 Our results suggested low storage temperature, the presence of calcium and low pH condition can make high-protein food products containing alpha-lactalbumin more stable. Calcium 63-70 lactalbumin alpha Homo sapiens 139-156 21524506-5 2011 A new and simple 2-step method for purification of calcium-free alpha-lactalbumin has been developed, and the resulting highly purified preparation was used to generate a complex with oleic acid. Calcium 51-58 lactalbumin alpha Homo sapiens 64-81 21524506-2 2011 An entirely different activity has been shown to occur when a complex is formed between calcium-free alpha-lactalbumin and oleic acid. Calcium 88-95 lactalbumin alpha Homo sapiens 101-118 20449034-7 2009 Upon binding of calcium to alpha-lactalbumin both the interaction and orientational alignment with lysozyme are reduced due to induced changes in the whey protein charge distribution. Calcium 16-23 lactalbumin alpha Homo sapiens 27-44 22016817-1 2011 BACKGROUND: Alpha-lactalbumin (alpha-LA) is a calcium-bound mammary gland-specific protein that is found in milk. Calcium 46-53 lactalbumin alpha Homo sapiens 12-29 22016817-1 2011 BACKGROUND: Alpha-lactalbumin (alpha-LA) is a calcium-bound mammary gland-specific protein that is found in milk. Calcium 46-53 lactalbumin alpha Homo sapiens 31-39 22016817-3 2011 When calcium is removed from alpha-LA, it adopts a molten globule form, and this form, interestingly, when complexed with oleic acid (OA) acquires tumoricidal activity. Calcium 5-12 lactalbumin alpha Homo sapiens 29-37 20416878-4 2010 Based on the analysis, calcium independent hydrophobic interaction chromatography was selected for separation of recombinant human alpha-lactalbumin (rHLA) from BLA in transgenic bovine milk. Calcium 23-30 lactalbumin alpha Homo sapiens 131-148 20449034-8 2009 This potentially explains the experimentally observed absence of supramolecular structuring for the calcium loaded holo alpha-lactalbumin. Calcium 100-107 lactalbumin alpha Homo sapiens 120-137 15659367-3 2005 The largest difference is seen for thermal denaturation of the calcium free (apo) forms, where the temperature at the transition midpoint is 15 degrees C lower for apo HAMLET than for apo alpha-lactalbumin. Calcium 63-70 lactalbumin alpha Homo sapiens 188-205 18620538-5 2008 These results demonstrate that the conformational change induced in alpha-lactalbumin by the removal of calcium enables the protein to interact with fatty acids. Calcium 104-111 lactalbumin alpha Homo sapiens 68-85 15822935-10 2005 The conformational state of alpha-lactalbumin in a complex with poly-Lys(Arg), named alpha-LActalbumin Modified by Poly-Amino acid (LAMPA), differs from all other alpha-lactalbumin states characterized to date, representing an apo-like (molten globule-like) state with substantially decreased affinity for calcium ion. Calcium 306-313 lactalbumin alpha Homo sapiens 28-45 15822935-10 2005 The conformational state of alpha-lactalbumin in a complex with poly-Lys(Arg), named alpha-LActalbumin Modified by Poly-Amino acid (LAMPA), differs from all other alpha-lactalbumin states characterized to date, representing an apo-like (molten globule-like) state with substantially decreased affinity for calcium ion. Calcium 306-313 lactalbumin alpha Homo sapiens 85-102 17260954-2 2007 As assessed by isothermal titration calorimetry, lysozyme did not bind to the native form of alpha-lactalbumin but did interact with calcium-depleted alpha-lactalbumin (apo alpha-LA). Calcium 133-140 lactalbumin alpha Homo sapiens 150-167 12651130-1 2003 Hydrogen exchange (HX) detected by mass spectrometry (MS) was used to analyze the structure of calcium-free alpha-lactalbumin, a model protein with marginal stability. Calcium 95-102 lactalbumin alpha Homo sapiens 108-125 12716681-3 2003 alpha-Lactalbumin, a major breast-milk protein, may contribute to a balanced amino acid pattern and increase calcium and zinc absorption. Calcium 109-116 lactalbumin alpha Homo sapiens 0-17 11787673-8 2001 Further studies will identify the role of calcium in the bioactivity of alpha-lactalbumin. Calcium 42-49 lactalbumin alpha Homo sapiens 72-89 11302449-2 2001 The theoretical electrophoretic mobility of globular proteins lysozyme and alpha-lactalbumin (apo and holo (+1 calcium per molecule) forms) was compared with those measured by capillary electrophoresis in phosphate at pH 7.0, versus the ionic strength (I) in the range 0-0.775 mol L(-1). Calcium 111-118 lactalbumin alpha Homo sapiens 75-92 10195284-3 1999 Alpha-lactalbumin is a metallo-protein and binds calcium, where as, only a few of the LYZs bind calcium. Calcium 49-56 lactalbumin alpha Homo sapiens 0-17 10625432-1 2000 Stopped-flow Fourier-transform infrared spectroscopy (SF-FTIR) was used to identify native as well as non-native secondary structures during the refolding of the calcium-binding protein alpha-lactalbumin. Calcium 162-169 lactalbumin alpha Homo sapiens 186-203 9537992-0 1998 Structural evidence for the presence of a secondary calcium binding site in human alpha-lactalbumin. Calcium 52-59 lactalbumin alpha Homo sapiens 82-99 9537992-1 1998 The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far. Calcium 122-129 lactalbumin alpha Homo sapiens 53-70 9537992-1 1998 The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far. Calcium 154-161 lactalbumin alpha Homo sapiens 53-70 9537992-1 1998 The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far. Calcium 154-161 lactalbumin alpha Homo sapiens 238-255 9537992-1 1998 The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far. Calcium 154-161 lactalbumin alpha Homo sapiens 53-70 9537992-1 1998 The high-resolution X-ray crystal structure of human alpha-lactalbumin (at 1.8 A) in the presence of an elevated level of calcium reveals a new secondary calcium binding site, 7.9 A away from the primary calcium binding site known in all alpha-lactalbumin structures so far. Calcium 154-161 lactalbumin alpha Homo sapiens 238-255 9537992-7 1998 The proximity of the manganese and calcium binding region and the location of the functional site on one side of the charged surface of the alpha-lactalbumin molecule suggest that these binding sites might play a role in the formation of the lactose synthase complex. Calcium 35-42 lactalbumin alpha Homo sapiens 140-157 2042737-2 1991 Detection of the calcium-binding proteins calmodulin and alpha-lactalbumin displays similar improvement, some other small proteins show slightly improved detection, while other proteins, especially those greater than or equal to 30 kDa, show none. Calcium 17-24 lactalbumin alpha Homo sapiens 57-74 9761690-1 1998 alpha-Lactalbumin, a small calcium-binding protein, forms an equilibrium molten globule state under a variety of conditions. Calcium 27-34 lactalbumin alpha Homo sapiens 0-17 7629032-1 1995 The high-affinity calcium-binding sites of bovine and human alpha-lactalbumin as well as equine lysozyme were analyzed by 113Cd NMR spectroscopy. Calcium 18-25 lactalbumin alpha Homo sapiens 60-77 7945790-10 1994 Fluorescence energy transfer measurements between Tb3+ in the strong calcium site to Co2+ in the strong Zn2+ site gave a distance in the range of 14-18 A, which was in excellent agreement with recent crystallographic data for human alpha-lactalbumin [Ren et al. Calcium 69-76 lactalbumin alpha Homo sapiens 232-249 1637811-7 1992 Competition experiments with EDTA showed that the affinities of these proteins for calcium follow the series bovine alpha-lactalbumin approximately human alpha-lactalbumin greater than pigeon lysozyme greater than equine lysozyme (KD approximately 5 x 10(-8) to 10(-6) M). Calcium 83-90 lactalbumin alpha Homo sapiens 154-171 18642242-4 1997 alpha-LA is a calcium metallo-protein and its isoelectric precipitation is governed by the protein-calcium complexation equilibrium. Calcium 14-21 lactalbumin alpha Homo sapiens 0-8 8547266-0 1996 Disulfide determinants of calcium-induced packing in alpha-lactalbumin. Calcium 26-33 lactalbumin alpha Homo sapiens 53-70 8547266-2 1996 Calcium binding to the wild-type alpha-LA molten globule induces a transition to the native state. Calcium 0-7 lactalbumin alpha Homo sapiens 33-41 8547266-3 1996 Here we assess the calcium-binding properties of the alpha-LA molten globule by studying two variants of alpha-LA. Calcium 19-26 lactalbumin alpha Homo sapiens 53-61 8547266-3 1996 Here we assess the calcium-binding properties of the alpha-LA molten globule by studying two variants of alpha-LA. Calcium 19-26 lactalbumin alpha Homo sapiens 105-113 8547266-5 1996 We found that only alpha-LA(beta) binds calcium, leading to the cooperative formation of substantial tertiary interactions. Calcium 40-47 lactalbumin alpha Homo sapiens 19-27 8547266-7 1996 Thus, specific interactions within alpha-LA imposed by the beta-sheet domain and interdomain disulfide bonds, as opposed to the two alpha-helical domain disulfides, are necessary for the calcium-induced progression from the molten globule toward more native-like structure. Calcium 187-194 lactalbumin alpha Homo sapiens 35-43 8547266-8 1996 Our results suggest that organization of the beta-sheet domain, coupled with calcium binding, comprises the locking step in the folding of alpha-LA from the molten globule to the native state. Calcium 77-84 lactalbumin alpha Homo sapiens 139-147 18623384-0 1995 Thermal isoelectric precipitation of alpha-lactalbumin from a whey protein concentrate: Influence of protein-calcium complexation. Calcium 109-116 lactalbumin alpha Homo sapiens 37-54 18623384-2 1995 As precipitation is a phenomenon dependent on the protein hydrophobicity, and as the release of the tightly bound calcium occurring at pH around 4 modifies the alpha-LA hydrophobicity, the specific role of calcium on isoelectric precipitation is investigated. Calcium 114-121 lactalbumin alpha Homo sapiens 160-168 18623384-3 1995 A study of the extent of alpha-LA precipitation in a whey protein concentrate under various operating conditions of pH, temperature, protein concentration, and calcium content is presented. Calcium 160-167 lactalbumin alpha Homo sapiens 25-33 2059662-0 1991 Calcium-regulated interactions of human alpha-lactalbumin with bee venom melittin. Calcium 0-7 lactalbumin alpha Homo sapiens 40-57 2628439-0 1989 Phylogenetic variations in the calcium-dependent electrophoretic shift of alpha-lactalbumin. Calcium 31-38 lactalbumin alpha Homo sapiens 74-91 34600648-0 2021 Enthalpy-entropy compensation in calcium binding to acid-base forms of glycine tyrosine dipeptides from hydrolysis of alpha-lactalbumin. Calcium 33-40 lactalbumin alpha Homo sapiens 118-135 2628439-1 1989 alpha-Lactalbumin undergoes a calcium-dependent electrophoretic shift at pH 8.3. Calcium 30-37 lactalbumin alpha Homo sapiens 0-17 2731545-2 1989 alpha-Lactalbumin evolved from the calcium-binding lysozyme along the mammalian lineage after the divergence of birds and mammals. Calcium 35-42 lactalbumin alpha Homo sapiens 0-17 2912378-3 1989 The existence of a high affinity binding site (Kdiss = 0.16 microM) (site I) for calcium ion in alpha-lactalbumin was confirmed by chromatography of [45Ca2+]. Calcium 81-88 lactalbumin alpha Homo sapiens 96-113 3167108-0 1988 [The effect of calcium and magnesium ions on the interaction of calcium-binding proteins parvalbumin and alpha-lactalbumin with dipalmitoylphosphatidylcholine vesicles]. Calcium 15-22 lactalbumin alpha Homo sapiens 105-122 3144978-4 1988 In order for a shift to be observed between the apo and calcium bound protein, calcium ion binding to proteins must have minimal dissociation constants (Kdiss) of 10(-7) M; alpha-lactalbumin is reported to bind calcium at Kdiss = 10(-10) to 10(-12) M. The electrophoretic shift identifies alpha-lactalbumin in complex milk whey patterns of many species of mammals. Calcium 79-86 lactalbumin alpha Homo sapiens 289-306 3144978-0 1988 The calcium-dependent electrophoretic shift of alpha-lactalbumin, the modifier protein of galactosyl transferase. Calcium 4-11 lactalbumin alpha Homo sapiens 47-64 3144978-3 1988 However, we detected the calcium shift for alpha-lactalbumin using non-denaturing PAGE (ND-PAGE) where electrical charge changes are observed upon binding calcium. Calcium 25-32 lactalbumin alpha Homo sapiens 43-60 3144978-3 1988 However, we detected the calcium shift for alpha-lactalbumin using non-denaturing PAGE (ND-PAGE) where electrical charge changes are observed upon binding calcium. Calcium 155-162 lactalbumin alpha Homo sapiens 43-60 3144978-4 1988 In order for a shift to be observed between the apo and calcium bound protein, calcium ion binding to proteins must have minimal dissociation constants (Kdiss) of 10(-7) M; alpha-lactalbumin is reported to bind calcium at Kdiss = 10(-10) to 10(-12) M. The electrophoretic shift identifies alpha-lactalbumin in complex milk whey patterns of many species of mammals. Calcium 56-63 lactalbumin alpha Homo sapiens 173-190 3144978-4 1988 In order for a shift to be observed between the apo and calcium bound protein, calcium ion binding to proteins must have minimal dissociation constants (Kdiss) of 10(-7) M; alpha-lactalbumin is reported to bind calcium at Kdiss = 10(-10) to 10(-12) M. The electrophoretic shift identifies alpha-lactalbumin in complex milk whey patterns of many species of mammals. Calcium 79-86 lactalbumin alpha Homo sapiens 173-190 3144978-4 1988 In order for a shift to be observed between the apo and calcium bound protein, calcium ion binding to proteins must have minimal dissociation constants (Kdiss) of 10(-7) M; alpha-lactalbumin is reported to bind calcium at Kdiss = 10(-10) to 10(-12) M. The electrophoretic shift identifies alpha-lactalbumin in complex milk whey patterns of many species of mammals. Calcium 79-86 lactalbumin alpha Homo sapiens 289-306 3144978-4 1988 In order for a shift to be observed between the apo and calcium bound protein, calcium ion binding to proteins must have minimal dissociation constants (Kdiss) of 10(-7) M; alpha-lactalbumin is reported to bind calcium at Kdiss = 10(-10) to 10(-12) M. The electrophoretic shift identifies alpha-lactalbumin in complex milk whey patterns of many species of mammals. Calcium 79-86 lactalbumin alpha Homo sapiens 173-190 3167108-0 1988 [The effect of calcium and magnesium ions on the interaction of calcium-binding proteins parvalbumin and alpha-lactalbumin with dipalmitoylphosphatidylcholine vesicles]. Calcium 64-71 lactalbumin alpha Homo sapiens 105-122 3657226-4 1987 These differences are in agreement with the chemical data about the interaction sites of both galactosyltransferase and calcium ions with alpha-lactalbumin, which are not required for the lysozyme function. Calcium 120-127 lactalbumin alpha Homo sapiens 138-155 3396853-0 1988 Interactions of calcium binding proteins, parvalbumin and alpha-lactalbumin, with dipalmitoylphosphatidylcholine vesicles. Calcium 16-23 lactalbumin alpha Homo sapiens 58-75 3558552-7 1986 Since alpha-LACT is a calcium binding protein, addition of this metal leads to stabilization, i.e. higher column temperatures are required for conformational change. Calcium 22-29 lactalbumin alpha Homo sapiens 6-16 32289905-5 2020 At a timescale of several nanoseconds, small differences in the amplitudes between the calcium enriched and depleted alpha-lactalbumin are visible, whereas at lower timescales no changes can be concluded within the statistics. Calcium 87-94 lactalbumin alpha Homo sapiens 117-134 3785375-0 1986 Alpha-lactalbumin possesses a novel calcium binding loop. Calcium 36-43 lactalbumin alpha Homo sapiens 0-17 3768320-1 1986 The distance between the calcium site (site I) and the zinc site (site II) in alpha-lactalbumin was estimated from Forster energy-transfer measurements between donor Eu(III) [or Tb(III)] at site I and acceptor Co(II) at site II to be 11.5 +/- 1.5 A. Intersite distances were also measured between the bis-ANS [4,4"-bis[1-(phenylamino)-8-naphthalenesulfonate]] binding locus and cobalt at site II (13.6 +/- 1.0 A), between bis-ANS and a fluorescein moiety covalently bound to Met-90 (33.5 +/- 3.0 A), and between Met-90 (fluorescein) and cobalt at site II (16.7 +/- 1.0 A). Calcium 25-32 lactalbumin alpha Homo sapiens 78-95 6789819-0 1981 Calcium binding to alpha-lactalbumin: structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes. Calcium 0-7 lactalbumin alpha Homo sapiens 19-36 3015998-7 1986 Lysozyme maintains a stable conformation over the temperature range 10-40 degrees C, whereas beta-lactoglobulin A has a conformational transition between 25 degrees C and 40 degrees C. Calcium-depleted alpha-lactalbumin, a rather labile species, maintains a stable conformation up to ca. Calcium 185-192 lactalbumin alpha Homo sapiens 202-219 3928842-0 1985 Calcium binding by alpha-lactalbumin in human milk and bovine milk. Calcium 0-7 lactalbumin alpha Homo sapiens 19-36 3928842-8 1985 Calcium binding was abolished at pH 3.0 and resulted in a substantial increase in the hydrodynamic radius of alpha-LA. Calcium 0-7 lactalbumin alpha Homo sapiens 109-117 6815244-0 1982 Identification of a calcium-binding protein in human milk as alpha-lactalbumin. Calcium 20-27 lactalbumin alpha Homo sapiens 61-78 32113138-0 2020 Influence of calcium fortification on physicochemical properties of whey protein concentrate solutions enriched in alpha-lactalbumin. Calcium 13-20 lactalbumin alpha Homo sapiens 115-132 30797338-4 2019 Molecular dynamic simulation and docking results demonstrated that the coil structures and locations, and the residues structures in the binding site of alpha-lactalbumin were affected, the binding site was the typical binding site of calcium ion and not changed during the processing. Calcium 235-242 lactalbumin alpha Homo sapiens 153-170 29916707-0 2018 Control of alpha-Lactalbumin Aggregation by Modulation of Temperature and Concentration of Calcium and Cysteine. Calcium 91-98 lactalbumin alpha Homo sapiens 11-28 28949782-1 2017 Alpha-lactalbumin (alpha-LA), a small milk calcium-binding globular protein, is known to possess noticeable anticancer activity, which is determined by the ability of this protein to form complexes with oleic acid (OA). Calcium 43-50 lactalbumin alpha Homo sapiens 0-17 28949782-1 2017 Alpha-lactalbumin (alpha-LA), a small milk calcium-binding globular protein, is known to possess noticeable anticancer activity, which is determined by the ability of this protein to form complexes with oleic acid (OA). Calcium 43-50 lactalbumin alpha Homo sapiens 19-27 28403179-1 2017 Nanotubes are formed by self-assembly of alpha-lactalbumin milk protein following a different route than established for the hydrolysis which involves V8 enzyme, phosphate buffer and appropriate amounts of calcium at neutral pH. Calcium 206-213 lactalbumin alpha Homo sapiens 41-58 27238572-3 2016 In this paper, we describe the peculiarities of metal binding to a multifunctional milk protein, alpha-lactalbumin, which has two domains, a large alpha-helical domain and a small beta-sheet domain connected by a calcium binding loop. Calcium 213-220 lactalbumin alpha Homo sapiens 97-114 27238572-7 2016 Besides canonical calcium binding, alpha-lactalbumin is known to interact with other metals, such as zinc (for which it has a specific binding site), and, in its apo-form, it can bind other divalent and monovalent cations. Calcium 18-25 lactalbumin alpha Homo sapiens 35-52