α‐lactalbumin: compact state with fluctuating tertiary structure?

Долгих, Д. А.; Gilmanshin, Rudolf; Бражников, Е. В.; Bychkova, Valentina E.; Semisotnov, Gennady V.; Venyaminov, Sergei Yu.; Ptitsyn, Oleg B.

doi:10.1016/0014-5793(81)80642-4

Cited by 619 publications

(455 citation statements)

References 21 publications

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“…At 270 nm, the bovine and caprine proteins showed the lowest minimum, while the equine and porcine spectra gave a weaker signal than human α-lactalbumin. The spectra of equine and porcine α-lactalbumin resembled the other species variants, as previously reported [8,12,[15][16][17][18][19]. The HAMLET-like complexes showed a loss of signal compared to each holo protein.…”

Section: Conversion Of the α-Lactalbumin Species Variants To Hamlet-lsupporting

confidence: 78%

“…Near UV CD spectra were recorded in 5 mM Tris, pH 7.0 on (A) human, equine, bovine, caprine and porcine α-lactalbumin and (B) HAMLET and HAMLETlike complexes. The spectra of human, bovine and caprine α-lactalbumins have previously been described [8,12,[15][16][17][18][19] but spectra of equine and porcine α-lactalbumin have not previously been reported. The L1210 mouse lymphoma cell line was exposed to (C) HAMLET and HAMLET-like complexes (0.2 mg/ml) or to (D) the corresponding native α-lactalbumin (0.5 mg/ml) for 5h.…”

Section: Can Hamlet-like Complexes Be Formed From Casein If Oleic Acimentioning

confidence: 99%

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α-Lactalbumin species variation, HAMLET formation, and tumor cell death

Pettersson

Mossberg

Svanborg

2006

Biochemical and Biophysical Research Communications

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HAMLET (human α-lactalbumin made lethal to tumor cells) is a tumoricidal complex of apo α-lactalbumin and oleic acid, formed in casein after low pH treatment of human milk. This study examined if HAMLET-like complexes are present in casein from different species and if isolated α-lactalbumin from those species can form such complexes with oleic acid. Casein from human, bovine, equine and porcine milk were separated by ion exchange chromatography and active complexes were only found in human casein. This was not explained by α-lactalbumin sequence variation, as purified bovine, equine, porcine and caprine α-lactalbumins formed complexes with oleic acid with biological activity similar to HAMLET. We conclude that structural variation of α-lactalbumins does not preclude the formation of HAMLET-like complexes and that natural HAMLET formation in casein was unique to human milk, which also showed the highest oleic acid content.

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Section: Conversion Of the α-Lactalbumin Species Variants To Hamlet-lsupporting

confidence: 78%

Section: Can Hamlet-like Complexes Be Formed From Casein If Oleic Acimentioning

confidence: 99%

α-Lactalbumin species variation, HAMLET formation, and tumor cell death

Pettersson

Mossberg

Svanborg

2006

Biochemical and Biophysical Research Communications

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“…Following previous researchers, 13 we suggested that disordered proteins could be either "extended" or "collapsed," 14 whereas others have pointed out data indicating the possibility of a third disorder class intermediate between extended and collapsed. 5 Collapsed disorder resembles the molten globule, 15 a protein form with regular secondary structure but absent of fixed tertiary interactions, and regions of extended disorder can also exhibit secondary structure. Thus, proteins or regions with regular secondary structure are not always ordered.…”

Section: Introductionmentioning

confidence: 99%

Flavors of protein disorder

et al. 2003

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Intrinsically disordered proteins are characterized by long regions lacking 3-D structure in their native states, yet they have been so far associated with 28 distinguishable functions. Previous studies showed that protein predictors trained on disorder from one type of protein often achieve poor accuracy on disorder of proteins of a different type, thus indicating significant differences in sequence properties among disordered proteins.

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“…Also, it would have an accessible hydrophobic core with increased fluctuations of side chains, a nearly native secondary structure and almost no tertiary structure. The MG state was first described for the proteins alactalbumin (5) and cytochrome c (6). Investigation of a-lactalbumin revealed that under certain denaturing conditions a stable intermediate state was formed which could be distinguished from the native and unfolded state.…”

Section: Introductionmentioning

confidence: 99%

Partially folded intermediates during trypsinogen denaturation

Martins

Santoro

1999

Braz J Med Biol Res

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The equilibrium unfolding of bovine trypsinogen was studied by circular dichroism, differential spectra and size exclusion HPLC. The change in free energy of denaturation was DG H 2 O = 6.99 ± 1.40 kcal/ mol for guanidine hydrochloride and DG H 2 O = 6.37 ± 0.57 kcal/mol for urea. Satisfactory fits of equilibrium unfolding transitions required a three-state model involving an intermediate in addition to the native and unfolded forms. Size exclusion HPLC allowed the detection of an intermediate population of trypsinogen whose Stokes radii varied from 24.1 ± 0.4 Å to 26.0 ± 0.3 Å for 1.5 M and 2.5 M guanidine hydrochloride, respectively. During urea denaturation, the range of Stokes radii varied from 23.9 ± 0.3 Å to 25.7 ± 0.6 Å for 4.0 M and 6.0 M urea, respectively. Maximal intrinsic fluorescence was observed at about 3.8 M urea with 8-aniline-1-naphthalene sulfonate (ANS) binding. These experimental data indicate that the unfolding of bovine trypsinogen is not a simple transition and suggest that the equilibrium intermediate population comprises one intermediate that may be characterized as a molten globule. To obtain further insight by studying intermediates representing different stages of unfolding, we hope to gain a better understanding of the complex interrelations between protein conformation and energetics.

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α‐lactalbumin: compact state with fluctuating tertiary structure?

Cited by 619 publications

References 21 publications

α-Lactalbumin species variation, HAMLET formation, and tumor cell death

α-Lactalbumin species variation, HAMLET formation, and tumor cell death

Flavors of protein disorder

Partially folded intermediates during trypsinogen denaturation

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