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Interaction of alph...
Interaction of alpha-lactalbumin with Cu2+.
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- Permyakov, E A (författare)
- Institute of Biological Physics, Pushchino, Russia
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- Morozova, L A (författare)
- Institute of Biological Physics, Pushchino, Russia
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Kalinichenko, L P (författare)
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visa fler...
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Derezhkov, V Yu (författare)
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visa färre...
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(creator_code:org_t)
- 1988
- 1988
- Engelska.
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Ingår i: Biophysical Chemistry. - 0301-4622 .- 1873-4200. ; 32:1, s. 37-42
- Relaterad länk:
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https://urn.kb.se/re...
Abstract
Ämnesord
Stäng
- It has been shown by intrinsic fluorescence spectroscopy that alpha-lactalbumin has several Cu2+ -binding sites per molecule. The Ca2+ -loaded protein binds two or more Cu2+ per molecule with an association constant of about 3 X 10(3) M-1. Apo-alpha-lactalbumin binds one Cu2+ per molecule with association constant 8 X 10(4) M-1 and from two to three Cu2+ with an association constant of about 4 X 10(3) M-1. The results obtained from spectrofluorometric pH titration of alpha-lactalbumin in the acidic pH region show the possible involvement of histidine residues in the coordination of Cu2+. The binding of Cu2+ to alpha-lactalbumin lowers significantly its thermostability and stability towards urea denaturation. The stability of Cu2+, Ca2+-alpha-lactalbumin against thermal and urea denaturation is similar to that of the apo protein. The thermal transition in Cu2+, Ca2+-alpha-lactalbumin occurs within the region of physiological temperatures which may suggest the existence of some thermal regulation of its functioning in vivo.
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