Distinct sites on the G-actin molecule bind group-specific component and deoxyribonuclease I

Pascal Goldschmidt-Clermont, R. M. Galbraith, D. L. Emerson, F. Marsot, A. E. Nel, P. Arnaud

Research output: Contribution to journalArticle

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Abstract

Addition of group-specific component (Gc) to G-actin with or without deoxyribonuclease I (DNAase) led to formation of binary complexes (Gc-G-actin) and ternary complexes (Gc-G-actin-DNAase) respectively. The electrophoretic mobility of ternary complexes, as shown by crossed and rocket immunoelectrophoresis, was slower than that of binary complexes, although both were faster than native Gc. In gradient polyacrylamide-gel electrophoresis, such complexes could again be resolved, apparently on the basis of relative molecular size: Gc-G-actin-DNAase (M(r) approx. 131,000), Gc-G-actin (M(r) approx. 98,000) and Gc (M(r) approx. 56,000). In contrast, the pI of ternary complex was indistinguishable by isoelectric focusing from that of binary complex, even though both were clearly more acidic than native Gc. The affinity of Gc for G-actin (affinity constant, K(a), 1.9x108 M-1) was not significantly altered by additional interaction with DNAase (K(a), 1.5x108 M-1), and both binary and ternary complexes still bound 25-hydroxycholecalciferol. In addition, the inhibitory effect of G-actin on DNAase activity was not discernibly affected by interaction with Gc. These results demonstrate that the various molecular forms of Gc can be distinguished by physicochemical parameters, and that Gc and DNAase bind to distinct sites on G-actin and can interact both independently and contemporaneously with this molecule.

Original languageEnglish
Pages (from-to)471-477
Number of pages7
JournalBiochemical Journal
Volume228
Issue number2
StatePublished - Aug 28 1985
Externally publishedYes

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Deoxyribonuclease I
Deoxyribonucleases
Actins
Molecules
Two-Dimensional Immunoelectrophoresis
Calcifediol
Myeloma Proteins
Electrophoretic mobility
Isoelectric Focusing
Rockets
Electrophoresis
Polyacrylamide Gel Electrophoresis

ASJC Scopus subject areas

  • Biochemistry

Cite this

Goldschmidt-Clermont, P., Galbraith, R. M., Emerson, D. L., Marsot, F., Nel, A. E., & Arnaud, P. (1985). Distinct sites on the G-actin molecule bind group-specific component and deoxyribonuclease I. Biochemical Journal, 228(2), 471-477.

Distinct sites on the G-actin molecule bind group-specific component and deoxyribonuclease I. / Goldschmidt-Clermont, Pascal; Galbraith, R. M.; Emerson, D. L.; Marsot, F.; Nel, A. E.; Arnaud, P.

In: Biochemical Journal, Vol. 228, No. 2, 28.08.1985, p. 471-477.

Research output: Contribution to journalArticle

Goldschmidt-Clermont, P, Galbraith, RM, Emerson, DL, Marsot, F, Nel, AE & Arnaud, P 1985, 'Distinct sites on the G-actin molecule bind group-specific component and deoxyribonuclease I', Biochemical Journal, vol. 228, no. 2, pp. 471-477.
Goldschmidt-Clermont P, Galbraith RM, Emerson DL, Marsot F, Nel AE, Arnaud P. Distinct sites on the G-actin molecule bind group-specific component and deoxyribonuclease I. Biochemical Journal. 1985 Aug 28;228(2):471-477.
Goldschmidt-Clermont, Pascal ; Galbraith, R. M. ; Emerson, D. L. ; Marsot, F. ; Nel, A. E. ; Arnaud, P. / Distinct sites on the G-actin molecule bind group-specific component and deoxyribonuclease I. In: Biochemical Journal. 1985 ; Vol. 228, No. 2. pp. 471-477.
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