A possible three-dimensional structure of bovine α-lactalbumin based on that of hen's egg-white lysozyme

Browne, W.J.; North, A. C. T.; Phillips, David; Brew, Keith; Vanaman, Thomas C.; Hill, Robert L.

doi:10.1016/0022-2836(69)90487-2

Cited by 503 publications

(118 citation statements)

References 13 publications

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“…It seems to be related to the evidence that polyglyc,)sylated lysozyme could be lethal to Gram-negative bacteria ilcluding Enterobacteriaceae following incubation at 50°C, bat could not be as lethal following incubation at 20°C [5]. I1~ addition, to verify the specific role of lysozyme in the conjt~gates, we used a-lactalbumin as a conjugate protein control, x~ hich has a close structural similarity to hen egg-white lysoz:..'me [17]. a-Lactalbumin conjugates did not exhibit any antinicrobial activities against E. tarda (data not shown).…”

Section: Resultsmentioning

confidence: 99%

Protective effect of lysozyme‐galactomannan or lysozyme‐palmitic acid conjugates against Edwardsiella tarda infection in carp, Cyprinus carpio L

et al. 1996

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The protective effect of lysozyme-galactomannan or lysozyme-palmitic acid conjugates orally administered to carp, Cyprinus carpio L. was investigated using a virulent strain of Gram-negative EdwardsieUa tarda isolated from an infected fish. Lysozyme-galactomannan conjugate was prepared through controlled Maillard reaction. Lysozyme-palmitic acid conjugate was prepared through base-catalyzed ester exchange using Nhydroxysuccinimide ester of palmitic acid. The conjugates provided substantial protection to carp infected with a Gramnegative bacteria f'Lsh pathogen E. tarda NG 8104. Lytic activities of lysozyme conjugates with galactomannan and palmitic acid were about 80 and 71% of native lysozyme using Micrococcus lysodeikticus as a substrate. Feeding with lysozyme conjugates, for 8 days, significantly enhanced fish protection against E. tarda infection. The survival rate was 30% for lysozyme-galactomannan conjugate treated fish and 20% for lysozyme-palmitic acid conjugate treated fish after 6 days cultivation while all control fish died within 3 days. On the other hand, a recovery rate of 40% after 6 days was observed in the fish group that were fed lysozyme-palmitic acid conjugate 3 and 2 h before and after E. tarda challenge, respectively, and for 6 consecutive days. The results of this work show the possibility of utilizing lysozyme conjugates with galactomannan or palmitic acid as a therapeutic for infection in fish.

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Section: Resultsmentioning

confidence: 99%

Protective effect of lysozyme‐galactomannan or lysozyme‐palmitic acid conjugates against Edwardsiella tarda infection in carp, Cyprinus carpio L

et al. 1996

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“…In the original comparative approach, a model is constructed from a few template core regions and from loops and side chains obtained from either aligned or unrelated structures. 4,10,11 Another family of comparative methods relies on approximate positions of conserved atoms from the templates to calculate the coordinates of other atoms. 12,13 A third group of methods uses either distance geometry or optimization techniques to satisfy spatial restraints obtained from the sequence-template alignment.…”

Section: Comparative Modeling and Threadingmentioning

confidence: 99%

Evolution and Physics in Comparative Protein Structure Modeling

et al. 2002

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From a physical perspective, the native structure of a protein is a consequence of physical forces acting on the protein and solvent atoms during the folding process. From a biological perspective, the native structure of proteins is a result of evolution over millions of years. Correspondingly, there are two types of protein structure prediction methods, de novo prediction and comparative modeling. We review comparative protein structure modeling and discuss the incorporation of physical considerations into the modeling process. A good starting point for achieving this aim is provided by comparative modeling by satisfaction of spatial restraints. Incorporation of physical considerations is illustrated by an inclusion of solvation effects into the modeling of loops.

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“…sharing similar primary, secondary, and tertiary structures (Brew et al, 1967;Browne et al, 1969;Stuart et al, 1986;Acharya et al, 1989Acharya et al, , 1991. Although it is generally accepted that a-LA evolved from C-type lysozyme, its function, i.e., in lactose synthesis, is clearly distinct from the lytic activity of its ancestral protein (McKenzie & White, 1991).…”

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confidence: 99%

Membrane‐bound states of α‐lactalbumin: Implications for the protein stability and conformation

1996

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Abstracta-Lactalbumin (a-LA) associates with dimyristoylphosphatidylcholine (DMPC) or egg lecithin (EPC) liposomes. Thermal denaturation of isolated DMPC or EPC a-LA complexes was dependent on the metal bound state of the protein. The intrinsic fluorescence of thermally denatured DMPC-a-LA was sensitive to two thermal transitions: the T,. of the lipid vesicles, and the denaturation of the protein. Quenching experiments suggested that tryptophan accessibility increased upon protein-DMPC association, in contrast with earlier suggestions that the limited emission red shift upon association with the liposome was due to partial insertion of tryptophan into the apolar phase of the bilayer (Hanssens I et al., 1985, Biochim Biophys Acta 817:154-166). On the other hand, above the protein transition (70 "C), the spectral blue shifts and reduced accessibility to quencher suggested that tryptophan interacts significantly with the apolar phase of either DMPC and EPC. At pH 2, where the protein inserts into the bilayer rapidly, the isolated DMPC-a-LA complex showed a distinct fluorescence thermal transition between 40 and 60 "C, consistent with a partially inserted form that possesses some degree of tertiary structure and unfolds cooperatively. This result is significant in light of earlier findings of increased helicity for the acid form, i.e., molten globule state of the protein (Hanssens I et al., 1985, Biochim Biophys Acta 812154-166). These results suggest a model where a limited expansion of conformation occurs upon association with the membrane at neutral pH and physiological temperatures, with a concomitant increase in the exposure of tryptophan to external quenchers; i.e., the current data do not support a model where an apolar, tryptophan-containing surface is covered by the lipid phase of the bilayer.

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A possible three-dimensional structure of bovine α-lactalbumin based on that of hen's egg-white lysozyme

Cited by 503 publications

References 13 publications

Protective effect of lysozyme‐galactomannan or lysozyme‐palmitic acid conjugates against Edwardsiella tarda infection in carp, Cyprinus carpio L

Protective effect of lysozyme‐galactomannan or lysozyme‐palmitic acid conjugates against Edwardsiella tarda infection in carp, Cyprinus carpio L

Evolution and Physics in Comparative Protein Structure Modeling

Membrane‐bound states of α‐lactalbumin: Implications for the protein stability and conformation

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