Surface and Spectroscopic Properties of Acetylcholinesterase Monolayer at the Air/Water Interface

Dziri, Leila; Puppala, Kalpama; Leblanc, Roger M.

doi:10.1006/jcis.1997.5069

Cited by 29 publications

(33 citation statements)

References 34 publications

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“…This may explain why the rate and/or extent of the adsorption of mtCK and MMCK are enhanced by an increase in ionic strength (0.3M NaCl) as it was the case for acetylcholinesterase. 65 Our data show that CK surface activity depends on its oligomeric state. When the mtCK octamer is FIGURE 9 Surface pressure-area isotherms recorded 3 h after spreading of 0.9 nM octameric mtCK onto a buffer containing Tris 20 mM, EDTA 0.1 mM, at pH 7.4 (~) or at pH 8.8 (^), or after spreading of 3.6 nM dimeric mtCK (n) onto a buffer at pH 8.8.…”

Section: Discussionmentioning

confidence: 92%

Interfacial behavior of cytoplasmic and mitochondrial creatine kinase oligomeric states

et al. 2005

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Adsorption to the air/water interface of isoenzymes of creatine kinase was investigated using surface pressure-area isotherms and Brewster angle microscopy (BAM) observations. Octameric mitochondrial creatine kinase (mtCK) exhibits a significant affinity for the air/water interface. Whatever the mode of formation of the interfacial film, i.e., injection of the protein in the subphase or spreading onto the buffer surface, the final arrangement and conformation adopted by mtCK molecules lead to a similar result. In contrast, the dimeric isoenzymes mtCK and cytosolic MMCK do not induce any surface pressure variation. However, when the subphase contains 0.3M NaCl, both isoenzymes adsorb to the interface. When treated with 0.8 or 3M GdnHCl, muscle creatine kinase (MMCK) becomes surface active and occupies a greater surface than mtCK. This result contrasts with previous observations, often derived from monomeric proteins, that their surface activity is increased upon unfolding. It underlines the possible influence exerted by the protein oligomeric state on its interfacial activity. At a subphase pH of 8.8, which corresponds to the pI of octameric mtCK, the profiles of the isotherms obtained with dimeric and octameric states and the resistance to compression of the protein monolayers are significantly affected when compared to those recorded at pH 7.4. These data suggest that the octamer is more hydrophobic than the dimer and may contribute to explaining why octamers bind to the inner mitochondrial membrane while dimers do not.

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Section: Discussionmentioning

confidence: 92%

Interfacial behavior of cytoplasmic and mitochondrial creatine kinase oligomeric states

et al. 2005

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“…The protein occupies larger areas on the electrolyte subphase, due to the decreased protein solubility in the bulk. Dziri et al observed a similar salting out effect for an acetylcholinesterase film on KCl subphases (1). Systematic studies of bull serum albumin monolayers on water and electrolyte subphases revealed increases in protein molecular areas on the surface of salt solutions (12).…”

Section: Factor I Penetration Of Lipid Monolayersmentioning

confidence: 92%

Association of Blood Clotting Factors I and VII with Phospholipid Monolayers at the Air–Water Interface

Serfis

Katzenberger

Williams

et al. 1999

Journal of Colloid and Interface Science

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“…Various studies reported in the literature that when aqueous solution of protein molecules spread on the water surface, some molecules sink into the bulk. However, the addition of electrolytes (salts) in the subphase has been a successful technique to reduce the solubility of protein in water and thus used for diminishing the amount of molecules that go under in the bulk, resulting in the configuration of more organized and stable monolayer at the air/water interface [35,36]. In that case, one should get true area/molecule.…”

Section: π -A Isotherm Studymentioning

confidence: 99%

Incorporation of ovalbumin within cationic octadecylamine monolayer and a comparative study with zwitterionic DPPC and anionic stearic acid monolayer

Kamilya

Pal

Talapatra

2007

Journal of Colloid and Interface Science

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Surface and Spectroscopic Properties of Acetylcholinesterase Monolayer at the Air/Water Interface

Cited by 29 publications

References 34 publications

Interfacial behavior of cytoplasmic and mitochondrial creatine kinase oligomeric states

Interfacial behavior of cytoplasmic and mitochondrial creatine kinase oligomeric states

Association of Blood Clotting Factors I and VII with Phospholipid Monolayers at the Air–Water Interface

Incorporation of ovalbumin within cationic octadecylamine monolayer and a comparative study with zwitterionic DPPC and anionic stearic acid monolayer

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