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Kinetics of inactivation of lectin: analysis of a method of tryptophan phosphorescence at room temperature

Mazhul', V.M.; Zaĭtseva, E.M.; Shavlovskiĭ, M.M.; Kuznetsova, I.M.; Turoverov, K.K.

Biofizika 48(5): 837-843

2003

ISSN/ISBN: 0006-3029
PMID: 14582408
Document Number: 559081
The internal dynamics of muscle actin during inactivation induced by guanidine hydrochloride (0.5-1.8 M) was studied by the method of room-temperature tryptophan phosphorescence (RTTP). It was shown that the essentially unfolded actin intermediate, which appears within the first minutes of incubation with guanidine hydrochloride, exhibits no RTTP, suggesting a high lability of its structure. Subsequent accumulation of associates of inactivated actin is accompanied by a significant increase in the intensity and decay time of RTTP, which is caused by the rigidity of the structure of inactivated actin. The kinetic dependencies of the intensity and lifetime of RTTP of actin during its inactivation depended on the concentration of the protein and guanidine hydrochloride.

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