## Abstract The interaction between tetrabromobisphenol A (TBBPA) and bovine serum albumin (BSA) in simulated physiological conditions (pHโ=โ7.4) was investigated by fluorescence spectroscopy. The results revealed that TBBPA caused the fluorescence quenching of BSA through a static quenching proced
Studies of polypeptide structure by fluorescence techniques. III. Interaction between dye and macromolecule in fluorescent conjugates
โ Scribed by Thomas J. Gill III; E. M. McLaughlin; Gilbert S. Omenn
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1967
- Tongue
- English
- Weight
- 675 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0006-3525
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โฆ Synopsis
Synopsis
'The effects of p11 on the polarization of flnoresrence of dyes dissolved in media of high visrosit y or conjugated to polypeptides that undergo no structural transitions indicate that DNS is useful for studying pH-dependent molecular transition over the range p H 2.5-14, whereas fluorescein is useful only over the range pH 6-8. Heating and cooling in aqueous solutions cause no change in the polarization of flnorescein or of DNS; there-* The nomenclature of the synthetic polypeptides was systematically defined previoiisly.~6 The snpersc4plh are lhe moliw pewelitage of each amino miid residue anti the nunil)er f o l l ~i ~i g f lie polypeptide fornmla tleiiotes the preparnt ioti. Other atitirevi:t-1 ions are PVAm, polyvin3.l:tmiiie; Fit(*, fliioresceiti isolhioc.3.a11:~te; I)NH, l-diniet hylaminonaphl hnleiie-5-sulfoityl chloride; 1)NS. S() ,TI, 1 -dimel 1~ylsm1iioriaphthaleiie-T,siilfonic acid; atid Iisec., natiosecoiid (lOP see.).
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